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5h34
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==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]] 1.75Å' 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> | ||
| + | </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> | ||
| + | <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'>[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. | ||
| + | <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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5h34" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | + | <references/> | |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Methionine--tRNA ligase]] | ||
| + | [[Category: Microarchaeum sp. kin4-m]] | ||
[[Category: Kaneko, A]] | [[Category: Kaneko, A]] | ||
| - | [[Category: Yoshida, H]] | ||
[[Category: Nambo, M]] | [[Category: Nambo, M]] | ||
| - | [[Category: | + | [[Category: Park, S Y]] |
[[Category: Suzuki, H]] | [[Category: Suzuki, H]] | ||
| + | [[Category: Tamura, K]] | ||
| + | [[Category: Umehara, T]] | ||
| + | [[Category: Yamamoto, T]] | ||
| + | [[Category: Yoshida, H]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Methionyl-trna synthetase]] | ||
| + | [[Category: Nanoarchaeum equitan]] | ||
| + | [[Category: Trna]] | ||
Revision as of 08:32, 16 November 2017
Crystal structure of the C-terminal domain of methionyl-tRNA synthetase (MetRS-C) in Nanoarchaeum equitans
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