Information on EC 6.1.1.11 - serine-tRNA ligase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

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EC NUMBER
COMMENTARY hide
6.1.1.11
-
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RECOMMENDED NAME
GeneOntology No.
serine-tRNA ligase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + L-serine + tRNASer = AMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
esterification
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-selenocysteine biosynthesis I (bacteria)
-
-
L-selenocysteine biosynthesis II (archaea and eukaryotes)
-
-
tRNA charging
-
-
selenocysteine biosynthesis
-
-
Aminoacyl-tRNA biosynthesis
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-serine:tRNASer ligase (AMP-forming)
This enzyme also recognizes tRNASec, the special tRNA for selenocysteine, and catalyses the formation of L-seryl-tRNASec, the substrate for EC 2.9.1.1, L-seryl-tRNASec selenium transferase.
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-48-7
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia
-
-
Manually annotated by BRENDA team
two isozymes through poylmorphism at position 197, L197S
UniProt
Manually annotated by BRENDA team
Escherichia coli B / ATCC 11303
B
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
C836
-
-
Manually annotated by BRENDA team
gene serS2
SwissProt
Manually annotated by BRENDA team
gene serS
SwissProt
Manually annotated by BRENDA team
strain ATCC 700974
UniProt
Manually annotated by BRENDA team
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
Uniprot
Manually annotated by BRENDA team
gene SerS
-
-
Manually annotated by BRENDA team
fragment; gene SerS
Q4CW46
SwissProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
-
impairment of zygotic Sars function leads to a significant dilatation of the aortic arch vessels and aberrant branching of cranial and intersegmental vessels
physiological function
additional information
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-dATP + L-serine + tRNASer
2'-dAMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
-
-
-
-
-
2-bromoadenosine 5'-triphosphate + L-serine + tRNASer
2-bromoadenosine 5'-monophosphate + diphosphate + L-seryl-tRNASer
show the reaction diagram
-
-
-
-
2-chloroadenosine 5'-triphosphate + L-serine + tRNASer
2-chloroadenosine 5'-monophosphate + diphosphate + L-seryl-tRNASer
show the reaction diagram
-
-
-
-
3'-NH2-ATP + L-serine + tRNASer
3'-NH2-AMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
-
-
-
-
ATP + DL-serine hydroxamate + tRNASer
?
show the reaction diagram
-
very weak activity
-
-
?
ATP + L-cysteine + tRNASer
AMP + diphosphate + L-cysteinyl-tRNASer
show the reaction diagram
-
very weak activity
-
-
?
ATP + L-serine + Fusaro tRNAPyl
AMP + diphosphate + L-seryl-Fusaro tRNAPyl
show the reaction diagram
-
Methanosarcina barkeri Fusaro tRNApyrrolysine (tRNAPyl) can be misacylated with serine by the Methanosarcina barkeri bacterial-type seryl-tRNA synthetase in vitro and in vivo in Escherichia coli. Compared to the Methanosarcina barkeri Fusaro tRNA, the Methanosarcina barkeri MS tRNAPyl contains two base changes: a G3:U70 pair
-
-
?
ATP + L-serine + tRNAPyl
AMP + diphosphate + L-seryl-tRNAPyl
show the reaction diagram
-
-
-
-
?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASe
show the reaction diagram
-
selenocysteine-incorporating tRNA wild-type and deletion mutants, secondary structures
-
?
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
show the reaction diagram
ATP + L-serine + tRNASecUCA
AMP + diphosphate + L-seryl-tRNASecUCA
show the reaction diagram
-
SerRS also aminoacylates tRNASec with serine as the first step for the incorporation of selenocysteine into proteins
-
-
?
ATP + L-serine + tRNASer
?
show the reaction diagram
-
-
-
-
-
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
ATP + L-serine + tRNASer (Escherichia coli)
AMP + diphosphate + L-seryl-tRNASer (Escherichia coli)
show the reaction diagram
-
-
-
-
?
ATP + L-serine + tRNASer (Saccharomyces cerevisiae)
AMP + diphosphate + L-seryl-tRNASer (Saccharomyces cerevisiae)
show the reaction diagram
-
-
-
-
?
ATP + L-serine + tRNASerCGA
AMP + diphosphate + L-seryl-tRNASerCGA
show the reaction diagram
-
-
-
-
?
ATP + L-serine + tRNASerGCU
AMP + diphosphate + L-seryl-tRNASerGCU
show the reaction diagram
ATP + L-serine + tRNASerUGA
AMP + diphosphate + L-seryl-tRNASerUGA
show the reaction diagram
ATP + L-threonine + tRNASer
AMP + diphosphate + L-threonyl-tRNASer
show the reaction diagram
-
very weak activity
-
-
?
dATP + L-serine + tRNASer
dAMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
-
-
-
-
-
formycin 5'-triphosphate + L-serine + tRNASer
formycin 5'-monophosphate + diphosphate + L-seryl-tRNASer
show the reaction diagram
-
-
-
-
additional information
?
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + L-serine + tRNASec
AMP + diphosphate + L-seryl-tRNASec
show the reaction diagram
ATP + L-serine + tRNASer
?
show the reaction diagram
-
-
-
-
-
ATP + L-serine + tRNASer
AMP + diphosphate + L-seryl-tRNASer
show the reaction diagram
additional information
?
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
-
50 mM, required for optimal activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(E)-3-(3-ethynyl-4-hydroxyphenyl)-1-(2-hydroxy-4-methoxy-3-(3-methylbut-2-en-1-yl)phenyl)prop-2-en-1-one
-
-
2-mercaptoethanol
-
-
4-hydroxyderricin
-
-
5'-O-[N-(L-Seryl)-sulfamoyl]adenosine
diphosphate
-
-
DL-Serine hydroxamate
GSSG
-
about 16% residual activity at 1 mM
Mg2+
-
inhibition by dead-end complex formation between the ternary complex, E-ATP-Ser, and either free Mg2+ or Mg2P2O7
p-hydroxymercuribenzoate
Phenylalanyl adenosine 5'-phosphate
-
-
Poly-arginine
-
-
serinamide
-
inhibition of methanogenic type seryl-tRNA synthetase, no inhibition of bacterial type seryl-tRNA synthetase
serine hydroxamate
serine methyl ester
-
-
Seryl adenosine 5'-phosphate
-
-
tRNASer-C-C
-
weak
-
tRNASer-C-C-3'dA
-
weak
-
tRNASer-C-C-Aoxi
-
weak
-
tRNASer-C-C-Foxi-red
-
weak
-
tRNASer-I-G-A oxidized with NaIO4
-
-
-
additional information
-
Trypanosoma brucei is highly sensitive to the action of specific selenoprotein inhibitors
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Intact SH-groups
-
required for activity
-
Pex21p
-
the enzyme interacts with the peroxisome biogenesis-related factor Pex21p, the C-terminally appended domain of yeast seryl-tRNA synthetase does not participate in substrate binding, but instead is required for association with Pex21p, Pex21p does not directly bind tRNA, and nor does it possess a tRNA-binding motif, but it instead participates in the formation of a specific ternary complex with seryl-tRNA synthetase and tRNASer, strengthening the interaction of seryl-tRNA synthetase with its cognate tRNASer, overview
-
tRNASer
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
2-Bromoadenosine 5'-triphosphate
-
-
0.05
2-Chloroadenosine 5'-triphosphate
-
-
1
3'-NH2-ATP
-
-
0.000068 - 0.55
ATP
0.00067
chloroplastic tRNASer from maize
-
mitochondrial isozyme, pH 7.5, 30°C
-
0.2
D-Ser
0.065
dATP
-
-
2.35
DL-Serine hydroxamate
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
2
Formycin 5'-triphosphate
-
-
29
L-cysteine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.0061 - 2.879
L-Ser
0.000104 - 0.9
L-serine
2 - 3.4
L-threonine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.00025
mitochondrial tRNASer from maize
-
mitochondrial isozyme, pH 7.5, 30°C
-
0.0004
mitochondrial tRNASer from yeast subtype 2
-
mitochondrial isozyme, pH 7.5, 30°C
-
0.00034 - 0.89
Ser
0.0033 - 0.031
tRNASec
-
0.004
tRNASec mutant without anticodon arm
-
pH 7.6, 37°C
-
0.0004
tRNASecUCA
-
pH 7.6, 37°C, recombinant enzyme
-
0.00004 - 1.191
tRNASer
0.000759
tRNASer (Escherichia coli)
-
at pH 7.5 and 30°C
-
0.000937
tRNASer (Saccharomyces cerevisiae)
-
at pH 7.5 and 30°C
-
0.0005
tRNASer from Escherichia coli
-
mitochondrial isozyme, pH 7.5, 30°C
-
0.0011
tRNASer mutant without anticodon arm
-
pH 7.6, 37°C
-
0.0029 - 0.003
tRNASer(CGA)
-
0.0013 - 0.0053
tRNASer(GCU)
-
0.0026 - 0.0047
tRNASer(GGA)
-
0.003
tRNASer-C-C-2'dA
-
-
-
0.0009
tRNASer-C-C-A
-
-
-
0.001
tRNASer-C-C-F
-
-
-
0.00125
tRNASer-CmCA
-
-
-
0.00084 - 0.0014
tRNASer-I-G-A
-
0.0032
tRNASerCGA
-
pH 7.6, 37°C, recombinant enzyme
-
0.35 - 0.37
tRNASerGCU
-
0.22 - 0.29
tRNASerUGA
-
additional information
additional information
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.031 - 6.08
ATP
0.9
chloroplastic tRNASer from maize
-
mitochondrial isozyme, pH 7.5, 30°C
-
2.433
DL-Serine hydroxamate
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.078
L-cysteine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.172 - 3.7
L-Ser
0.0014 - 7
L-serine
0.14
L-threonine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.2
mitochondrial tRNASer from maize
-
mitochondrial isozyme, pH 7.5, 30°C
-
0.5
mitochondrial tRNASer from yeast subtype 2
-
mitochondrial isozyme, pH 7.5, 30°C
-
0.03 - 3.8
Ser
0.833
SertRNASer
-
-
-
0.007 - 9.2
tRNASec
-
0.005
tRNASec mutant without anticodon arm
-
pH 7.6, 37°C
-
0.000000011 - 13.7
tRNASer
0.14
tRNASer (Escherichia coli)
-
at pH 7.5 and 30°C
-
0.13
tRNASer (Saccharomyces cerevisiae)
-
at pH 7.5 and 30°C
-
1.2
tRNASer from Escherichia coli
-
mitochondrial isozyme, pH 7.5, 30°C
-
0.023
tRNASer mutant without anticodon arm
-
pH 7.6, 37°C
-
1.07 - 3.05
tRNASer(CGA)
-
0.92 - 1.13
tRNASer(GCU)
-
0.9 - 4.4
tRNASer(GGA)
-
0.35 - 6.08
tRNASerGCU
-
0.63 - 6.08
tRNASerUGA
-
additional information
additional information
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.04
DL-Serine hydroxamate
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.0027
L-cysteine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
0.016 - 13.9
L-serine
0.006
L-threonine
-
in 50 mM HEPES pH 7.0, 25 mM KCl, 20 mM MgCl2, temperature not specified in the publication
298
tRNASec
-
at pH 7.6, temperature not specified in the publication
-
1275 - 1900
tRNASer
180
tRNASer (Escherichia coli)
-
at pH 7.5 and 30°C
-
140
tRNASer (Saccharomyces cerevisiae)
-
at pH 7.5 and 30°C
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 3.1
5'-O-[N-(L-Seryl)-sulfamoyl]adenosine
0.0032 - 1
serinamide
0.18 - 18.1
serine hydroxamate
0.55 - 3.5
serine methyl ester
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0238
(E)-3-(3-ethynyl-4-hydroxyphenyl)-1-(2-hydroxy-4-methoxy-3-(3-methylbut-2-en-1-yl)phenyl)prop-2-en-1-one
Staphylococcus aureus
-
in 100 mM HEPES (pH 7.2), 10 mM MgCl2, 30 mM KCl, at 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0068
-
purified mitochondrial isozyme
0.093
-
-
0.15
-
-
0.76
-
-
10.87
-
-
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1 - 8.1
-
in phosphate and Tris buffer
7.8
-
Hepes or Tris-HCl buffer
8.1
-
Hepes buffer
8.2 - 8.8
-
aminoacylation
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
25°C, acylation rate increases when pH is raised from 6.0 to 8.0
7.3 - 10
-
7.3: about 30% of maximal activity, 10: about 60% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
aminoacylation assay at room temperature
35
aminoacylation assay at
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
-
isoelectric focusing
7.9
-
isoelectric focusing
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
expression at low level
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
high expression
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
expression at low level
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
-
low expression
Manually annotated by BRENDA team
additional information
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
dual localization is established by the virtue of an ambiguous targeting peptid at the very N-terminus
Manually annotated by BRENDA team
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Aquifex aeolicus (strain VF5)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Methanosarcina barkeri (strain Fusaro / DSM 804)
Methanosarcina barkeri (strain Fusaro / DSM 804)
Methanosarcina barkeri (strain Fusaro / DSM 804)
Methanosarcina barkeri (strain Fusaro / DSM 804)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000
-
2 * 47000, sedimentation studies after dissociation in 6 M guanidine hydrochloride
48700
x * 48700, recombinant enzyme, SDS-PAGE
49000
-
2 * 49000, SDS-PAGE
55000
-
2 * 55000, SDS-PAGE
57000
-
2 * 57000, recombinant mitochondrial isozyme, SDS-PAGE
59000
-
SDS-PAGE
60000
-
2 * 60000, SDS-PAGE
81000
-
gel filtration, sedimentation velocity
87000
-
2 * 87000 (alpha), SDS-PAGE
88000
-
sedimentation equilibrium measurement
89000
-
equilibrium ultracentrifugation method
95000
-
sedimentation studies
100000
-
gel filtration
103000
-
meniscus depletion method
109000
-
recombinant mitochondrial isozyme, gel filtration
110000
-
gel filtration
114000
-
sucrose density gradient centrifugation
115000 - 154000
-
dynamic light scattering
124000
-
gel filtration, sedimentation velocity
170000
-
gel filtration
additional information
-
-
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
additional information
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of mtRS in complex with seryl adenylate at 1.65 A resolution, space group P222(1) with unit cell parameters a = 79.9, b = 230 A, c = 135.6 A
-
recombinant enzyme, hanging drop vapor-diffusion method. Crystals diffract well beyond a resolution of 1.16 A and belong to the orthorhombic space group C222(1), with unit cell parameters a = 79.89, b = 230.42, c = 13560. There is one dimer in the asymmetric unit, with a solvent content of 55%
-
sitting-drop vapour-diffusion method. Crystals grew in a very narrow range of conditions using PEG 8000 as precipitant at room temperature. An appropriate concentration of lithium sulfate was critical for crystal nucleation. Crystals diffracted well beyond a resolution of 1.6 A and were found to belong to the orthorhombic space group C222(1), with unit-cell parameters a = 79.89 A, b = 230.42 A, c = 135.60 A. There is one dimer in the asymmetric unit, with a solvent content of 55%
-
purified isozymes, sitting-drop vapour-diffusion method, 8-14 mg/ml protein in 50 mM Na HEPES, pH 7.6, 150 mM KCl, 10 mM MgCl2, and 8% v/v glycerol, is mixed with reservoir solution containing 100 mM Na MES pH 5.6-5.8, 3.2-3.4 M ammonium sulfate and 0-2% v/v glycerol, equilibration against 0.5 ml of reservoir solution. Binary complexes SerRS-SerSA and SerRS-ATP, SerRS_Ser197 with 15 mM 5'-O-[N-(l-seryl)sulfamoyl]adenosine or 10 mM ATP, are mixed with 100 mM Na MES pH 5.8-6.2, 3.3-3.4 M ammonium sulfate and 0-5% v/v glycerol as precipitant solution, 2-3 days, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement for analysis of crystal structures of unliganded SerRS and of its complexes with ATP and with a seryl-adenylate analogue
in complex with 5'-O-(N-(L-seryl)-sulfamoyl)adenosine, sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M ammonium fluoride or ammonium formate, and 0.1 M HEPES pH 7.0
-
mutant enzymes E447K and E156T/R157S, sitting drop vapor diffusion method, using 12% (w/v) PEG 3350, 0.2 M NaCl and 0.1 MTris-HCl (pH 7.5)
-
purified hsSerRS, sitting-drop vapour diffusion method, 0.01875 ml of protein solution containing 10 mg/ml protein in HCl, pH 7.9, 100 mM NaCl, 10 mM MgCl2, 5% glycerol, 5 mM DTT, with 0.00625 ml of reservoir solution containing 100 mM ammonium sulfate, 22% w/v PEG 3350, 5% glycerol, 200 mM sodium formate pH 7.2, supplemented with 20% v/v glycerol, and equilibration against 0.5 ml of reservoir solution, 12°C, 2 weeks, X-ray diffraction structure determination and analysis at 3.1 A resolution
-
in complex with tRNASec from Aquifex aeolicus, sitting drop vapor diffusion method, using 100 mM trisodium citrate-HCl buffer pH 5.6 containing 2.0 M ammonium sulfate and 200 mM potassium sodium tartrate
-
SerRS free and in complex with ATP, serine and the nonhydrolysable seryl-adenylate analogue 5'-O-(N-serylsulfamoyl) adenosine, X-ray diffraction structure determination and anaylsis at 2.5 A resolution
-
crystal structures of the SerRS from the archaeon Pyrococcus horikoshii bound with 5'-O-[N-(L-seryl)-sulfamoyl]-adenosine are solved at 2.6 A, with ATP at 2.8 A, and in the apo form at 3.0 A. SerRS recognizes the seryl and adenylate moieties in a manner similar to those of the bacterial and mitochondrial SerRSs from Thermus ther