Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Jurgenson, C.T.; Burns, K.E.; Begley, T.P.; Ealick, S.E.
    Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis (2008), Biochemistry, 47, 10354-10364.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.5.1.65 expressed in Escherichia coli as a His-tagged fusion protein Mycobacterium tuberculosis
2.5.1.113 expressed in Escherichia coli B834(DE3) and BL21(DE3) cells Mycobacterium tuberculosis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.5.1.65 the structure of the protein complex CysM-CysO is determined at 1.53 A resolution. The protein complex in the crystal structure is asymmetric with one CysO (sulfur carrier protein) protomer binding to one end of a CysM dimer. The structures of CysM is determined individually at 2.8 A resolution. Sequence alignments with homologues and structural comparisons with CysK, a cysteine synthase that does not utilize a sulfur carrier protein, reveal high conservation of active site residues, but residues in CysM responsible for CysO binding are not conserved Mycobacterium tuberculosis
2.5.1.113 native enzyme bound to CysO sulfur-carrier protein, hanging drop vapor diffusion method, using 7-10% PEG (w/v) 4000, 0.1 M sodium citrate, pH 5.8, and 0.2 M ammonium acetate at 22°C Mycobacterium tuberculosis

Protein Variants

EC Number Protein Variants Comment Organism
2.5.1.65 K204A to improve crystallization of CysM alone, a putative surface residue in CysM (Lys204) is mutated to alanine using site-directed mutagenesis Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.5.1.113 O-acetyl-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH Mycobacterium tuberculosis
-
 [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + acetate
-
 ?
2.5.1.113 O-acetyl-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH Mycobacterium tuberculosis H37Rv
-
 [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.5.1.65 Mycobacterium tuberculosis
-
-
-
2.5.1.113 Mycobacterium tuberculosis
-
-
-
2.5.1.113 Mycobacterium tuberculosis H37Rv
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.5.1.65 using Ni-NTA chromatography Mycobacterium tuberculosis
2.5.1.113 Ni-NTA column chromatography Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.5.1.113 O-acetyl-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
-
 Mycobacterium tuberculosis [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + acetate
-
 ?
2.5.1.113 O-acetyl-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH
-
 Mycobacterium tuberculosis H37Rv [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + acetate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.5.1.65 dimer crystal structure Mycobacterium tuberculosis
2.5.1.113 homodimer x-ray crystallography Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.5.1.65 CysM
-
 Mycobacterium tuberculosis
2.5.1.65 Rv1336
-
 Mycobacterium tuberculosis
2.5.1.113 CysM
-
 Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.5.1.65 pyridoxal 5'-phosphate
-
 Mycobacterium tuberculosis
2.5.1.113 pyridoxal 5'-phosphate
-
 Mycobacterium tuberculosis