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5h34

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Crystal structure of the C-terminal domain of methionyl-tRNA synthetase (MetRS-C) in Nanoarchaeum equitans

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 ==Crystal structure of the C-terminal domain of methionyl-tRNA synthetase (MetRS-C) in Nanoarchaeum equitans==
-<StructureSection load='5h34' size='340' side='right' caption='[[5h34]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+<StructureSection load='5h34' size='340' side='right'caption='[[5h34]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5h34]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Microarchaeum_sp._kin4-m Microarchaeum sp. kin4-m]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H34 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H34 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5h34]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nanoarchaeum_equitans_Kin4-M Nanoarchaeum equitans Kin4-M]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H34 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">metG, NEQ457 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=228908 Microarchaeum sp. Kin4-M])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.748&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine--tRNA_ligase Methionine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.10 6.1.1.10] </span></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=5h34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h34 OCA], [https://pdbe.org/5h34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h34 RCSB], [https://www.ebi.ac.uk/pdbsum/5h34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h34 ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5h34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h34 OCA], [http://pdbe.org/5h34 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h34 RCSB], [http://www.ebi.ac.uk/pdbsum/5h34 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h34 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SYM_NANEQ SYM_NANEQ]] Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
+[https://www.uniprot.org/uniprot/SYM_NANEQ SYM_NANEQ] Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The C-terminal domain of methionyl-tRNA synthetase (MetRS-C) from Nanoarchaeum equitans is homologous to a tRNA-binding protein consisting of 111 amino acids (Trbp111) from Aquifex aeolicus. The crystal structure of MetRS-C showed that it existed as a homodimer, and that each monomer possessed an oligonucleotide/oligosaccharide-binding fold (OB-fold). Analysis using a quartz crystal microbalance indicated that MetRS-C freshly isolated from N. equitans was bound to tRNA. However, binding of the split 3'-half tRNA species was stronger than that of the 5'-half species. The T-loop and the 3'-end regions of the split 3'-half tRNA were found to be responsible for the binding. The minimum structure for binding to MetRS-C might be a minihelix-like stem-loop with single-stranded 3'-terminus. After successive duplications of such a small hairpin structure with the assistance of a Trbp-like structure, the interaction of the T-loop region of the 3'-half with a Trbp-like structure could have been evolutionarily replaced by RNA-RNA interactions, along with many combinational tertiary interactions, to form the modern tRNA structure.
-Binding Properties of Split tRNA to the C-terminal Domain of Methionyl-tRNA Synthetase of Nanoarchaeum equitans.,Suzuki H, Kaneko A, Yamamoto T, Nambo M, Hirasawa I, Umehara T, Yoshida H, Park SY, Tamura K J Mol Evol. 2017 Jun;84(5-6):267-278. doi: 10.1007/s00239-017-9796-6. Epub 2017, Jun 6. PMID:28589220<ref>PMID:28589220</ref>
+==See Also==
+*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5h34" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Methionine--tRNA ligase]]
+[[Category: Large Structures]]
-[[Category: Microarchaeum sp. kin4-m]]
+[[Category: Nanoarchaeum equitans Kin4-M]]
-[[Category: Kaneko, A]]
+[[Category: Kaneko A]]
-[[Category: Nambo, M]]
+[[Category: Nambo M]]
-[[Category: Park, S Y]]
+[[Category: Park SY]]
-[[Category: Suzuki, H]]
+[[Category: Suzuki H]]
-[[Category: Tamura, K]]
+[[Category: Tamura K]]
-[[Category: Umehara, T]]
+[[Category: Umehara T]]
-[[Category: Yamamoto, T]]
+[[Category: Yamamoto T]]
-[[Category: Yoshida, H]]
+[[Category: Yoshida H]]
-[[Category: Ligase]]
-[[Category: Methionyl-trna synthetase]]
-[[Category: Nanoarchaeum equitan]]
-[[Category: Trna]]

5h34

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Crystal structure of the C-terminal domain of methionyl-tRNA synthetase (MetRS-C) in Nanoarchaeum equitans

Structural highlights

Function

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