View source for 7eiv


==heterotetrameric glycyl-tRNA synthetase from Escherichia coli==
<StructureSection load='7eiv' size='340' side='right'caption='[[7eiv]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7eiv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EIV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EIV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=7eiv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eiv OCA], [https://pdbe.org/7eiv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eiv RCSB], [https://www.ebi.ac.uk/pdbsum/7eiv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eiv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SYGA_ECOLI SYGA_ECOLI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
AaRSs (aminoacyl-tRNA synthetases) group into two ten-member classes throughout evolution, with unique active site architectures defining each class. Most are monomers or homodimers but, for no apparent reason, many bacterial GlyRSs are heterotetramers consisting of two catalytic alpha-subunits and two tRNA-binding beta-subunits. The heterotetrameric GlyRS from Escherichia coli (EcGlyRS) was historically tested whether its alpha- and beta-polypeptides, which are encoded by a single mRNA with a gap of three in-frame codons, are replaceable by a single chain. Here, an unprecedented X-shaped structure of EcGlyRS shows wide separation of the abutting chain termini seen in the coding sequences, suggesting strong pressure to avoid a single polypeptide format. The structure of the five-domain beta-subunit is unique across all aaRSs in current databases, and structural analyses suggest these domains play different functions on alpha-subunit binding, ATP coordination and tRNA recognition. Moreover, the X-shaped architecture of EcGlyRS largely fits with a model for how two classes of tRNA synthetases arose, according to whether enzymes from opposite classes can simultaneously co-dock onto separate faces of the same tRNA acceptor stem. While heterotetrameric GlyRS remains the last structurally uncharacterized member of aaRSs, our study contributes to a better understanding of this ancient and essential enzyme family.

X-shaped structure of bacterial heterotetrameric tRNA synthetase suggests cryptic prokaryote functions and a rationale for synthetase classifications.,Ju Y, Han L, Chen B, Luo Z, Gu Q, Xu J, Yang XL, Schimmel P, Zhou H Nucleic Acids Res. 2021 Sep 27;49(17):10106-10119. doi: 10.1093/nar/gkab707. PMID:34390350<ref>PMID:34390350</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7eiv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Ju Y]]
[[Category: Zhou H]]