1j09 Summary


Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with ATP and Glu

The structure was published by Sekine, S., Nureki, O., Dubois, D.Y., et al., Lapointe, J., Vassylyev, D.G., and Yokoyama, S., in 2003 in a paper entitled "ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2002.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Glutamyl-tRNA synthetase. This molecule has the UniProt identifier P27000 (SYE_THET8)search. The sample contained 468 residues which is 100% of the natural sequence. Out of 468 residues 468 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Glutamyl-tRNA synthetase P27000 (1-468) (SYE_THET8)search Thermus thermophilus HB8search 100% 468 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P27000 (1 - 468) Glutamyl-tRNA synthetase Thermus thermophilus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P27000) C-terminal domain of glutamyl-tRNA synthetase (GluRS)search, Class I aminoacyl-tRNA synthetases (RS), catalytic domainsearch HUPssearch, Glutamyl-trna Synthetase; Domain 2search, Glutamyl-tRNA Synthetase; Domain 3search, Helicase, Ruva Protein; domain 3search, Arc Repressor Mutant, subunit Asearch PF00749: tRNA synthetases class I (E and Q), catalytic domainsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P27000) tRNA aminoacylationsearch glutamyl-tRNA aminoacylationsearch tRNA aminoacylation for protein translationsearch translationsearch glutamate-tRNA ligase activitysearch ATP bindingsearch nucleotide bindingsearch aminoacyl-tRNA ligase activitysearch ligase activity, forming aminoacyl-tRNA and related compoundssearch tRNA bindingsearch ligase activitysearch cytoplasmsearch

Chain InterPro annotation
A Glutamyl/glutaminyl-tRNA synthetasesearch Aminoacyl-tRNA synthetase, class I, conserved sitesearch Glutamate-tRNA ligase, bacterial/mitochondrialsearch Aminoacyl-tRNA synthetase, class I, anticodon-bindingsearch Rossmann-like alpha/beta/alpha sandwich foldsearch Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domainsearch Glutamyl/glutaminyl-tRNA synthetase, class Ib, alpha-bundle domainsearch Aminoacyl-tRNA synthetase, class I, anticodon-binding domain, subdomain 2search Aminoacyl-tRNA synthetase, class I, anticodon-binding domain, subdomain 1search