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Literature summary for 6.1.1.1 extracted from

  • Mykuliak, V.V.; Dragan, A.I.; Kornelyuk, A.I.
    Structural states of the flexible catalytic loop of M. tuberculosis tyrosyl-tRNA synthetase in different enzyme-substrate complexes (2014), Eur. Biophys. J., 43, 613-622 .
    View publication on PubMed
Search for more literature for 6.1.1.1

Application

Application Comment Organism
drug development the enzyme is a promising target for development of novel selective inhibitors as putative antituberculosis drugs Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
additional information prevention of beta-sheet formation by introducing point mutations in the loop sequence results in a rapid transition (below 20 ns) of the loop from its functional closed M-like structure to an inactive open O-like structure, i.e. rapid diffusion of the catalytic loop outside the active site Mycobacterium tuberculosis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-tyrosine + tRNATyr Mycobacterium tuberculosis
-
 AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
ATP + L-tyrosine + tRNATyr Mycobacterium tuberculosis ATCC 25618
-
 AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
additional information Mycobacterium tuberculosis enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr ?
-
 ?
additional information Mycobacterium tuberculosis ATCC 25618 enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WFT1
-
-
Mycobacterium tuberculosis ATCC 25618 P9WFT1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-tyrosine + tRNATyr
-
 Mycobacterium tuberculosis AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
ATP + L-tyrosine + tRNATyr
-
 Mycobacterium tuberculosis ATCC 25618 AMP + diphosphate + L-tyrosyl-tRNATyr
-
 ?
additional information enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr Mycobacterium tuberculosis ?
-
 ?
additional information enzyme MtTyrRS is incapable of cross-recognition and aminoacylation of human cytoplasmic tRNATyr Mycobacterium tuberculosis ATCC 25618 ?
-
 ?

Subunits

Subunits Comment Organism
homodimer the MtTyrRS monomer contains three domains: the catalytic domain (1-248), the anticodon-binding domain (249-341), and the C-terminal domain (342-424), three-dimensional structure of the MtTyrRS dimer, overview Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
mtTyrRS
-
 Mycobacterium tuberculosis
Tyrosyl-tRNA synthetase
-
 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
evolution the enzyme belongs to class I of aminoacyl-tRNA synthetases Mycobacterium tuberculosis
additional information enzyme MtTyrRS contains the HIGH-like and KFGKS catalytic motifs that catalyze amino acid activation with ATP.The conformational mobility of MtTyrRS catalytic KFGKS loop is analyzed by 100-ns all-atoms molecular dynamics simulations of the free enzyme and its complexes with different substrates: tyrosine, ATP, and the tyrosyl-adenylate intermediate. In the closed state of the active site, the KFGKS loop, readily adopts different stable conformations depending on the type of bound substrate. The closed state of the loop is stabilized by dynamic formation of two antiparallel beta-sheets at flanking ends which hold the KFGKS fragment inside the active center. Molecular dynamics simulations, conformation of the MtTyrRS catalytic loop in substrate?bound states, detailed overview Mycobacterium tuberculosis
physiological function the flexibility and rapid dynamics of the wild-type aminoacyl-tRNA synthetase catalytic loop structure are crucial for formation of protein-substrate interactions and subsequently for overall enzyme functional activity, dynamic properties of the enzyme, overview Mycobacterium tuberculosis