1gln

<table><tr><td colspan='2'>[[1gln]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GLN FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gln OCA], [https://pdbe.org/1gln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gln RCSB], [https://www.ebi.ac.uk/pdbsum/1gln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gln ProSAT], [https://www.topsan.org/Proteins/RSGI/1gln TOPSAN]</span></td></tr>

[[https://www.uniprot.org/uniprot/SYE_THET8 SYE_THET8]] Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu).<ref>PMID:11224561</ref> <ref>PMID:17161369</ref>

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== Publication Abstract from PubMed ==

The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus, was solved and refined at 2.5 A resolution. The amino-terminal half of GluRS shows a geometrical similarity with that of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) of the same subclass in class I, comprising the class I-specific Rossmann fold domain and the intervening subclass-specific alpha/beta domain. These domains were found to have two GluRS-specific, secondary-structure insertions, which then participated in the specific recognition of the D and acceptor stems of tRNA(Glu) as indicated by mutagenesis analyses based on the docking properties of GluRS and tRNA. In striking contrast to the beta-barrel structure of the GlnRS carboxyl-terminal half, the GluRS carboxyl-terminal half displayed an all-alpha-helix architecture, an alpha-helix cage, and mutagenesis analyses indicated that it had a role in the anticodon recognition.

Architectures of class-defining and specific domains of glutamyl-tRNA synthetase.,Nureki O, Vassylyev DG, Katayanagi K, Shimizu T, Sekine S, Kigawa T, Miyazawa T, Yokoyama S, Morikawa K Science. 1995 Mar 31;267(5206):1958-65. PMID:7701318<ref>PMID:7701318</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1gln" style="background-color:#fffaf0;"></div>

[[Category: Thermus thermophilus]]

[[Category: Katayanagi, K]]

[[Category: Kigawa, T]]

[[Category: Miyazawa, T]]

[[Category: Morikawa, K]]

[[Category: Nureki, O]]

[[Category: Structural genomic]]

[[Category: Sekine, S]]

[[Category: Shimizu, T]]

[[Category: Vassylyev, D G]]

[[Category: Yokoyama, S]]

[[Category: Rsgi]]