View source for 5xgq


==Crystal structure of apo form (free-state) Mycobacterium tuberculosis methionyl-tRNA synthetase==
<StructureSection load='5xgq' size='340' side='right'caption='[[5xgq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xgq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Ra Mycobacterium tuberculosis H37Ra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XGQ 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]] 1.899&#8491;</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=5xgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xgq OCA], [https://pdbe.org/5xgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xgq RCSB], [https://www.ebi.ac.uk/pdbsum/5xgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xgq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A5U150_MYCTA A5U150_MYCTA] Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.[HAMAP-Rule:MF_01228]
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== Publication Abstract from PubMed ==
Mycobacterium tuberculosis (MTB) caused 10.4 million cases of tuberculosis and 1.7 million deaths in 2016. The incidence of multidrug-resistant and extensively drug-resistant MTB is becoming an increasing threat to public health and the development of novel anti-MTB drugs is urgently needed. Methionyl-tRNA synthetase (MetRS) is considered to be a valuable drug target. However, structural characterization of M. tuberculosis MetRS (MtMetRS) was lacking for decades, thus hampering drug design. Here, two high-resolution crystal structures of MtMetRS are reported: the free-state structure (apo form; 1.9 A resolution) and a structure with the intermediate product methionyl-adenylate (Met-AMP) bound (2.4 A resolution). It was found that free-state MtMetRS adopts a previously unseen conformation that has never been observed in other MetRS homologues. The pockets for methionine and AMP are not formed in free-state MtMetRS, suggesting that it is in a nonproductive conformation. Combining these findings suggests that MtMetRS employs an induced-fit mechanism in ligand binding. By comparison with the structure of human cytosolic MetRS, additional pockets specific to MtMetRS that could be used for anti-MTB drug design were located.

Structural characterization of free-state and product-state Mycobacterium tuberculosis methionyl-tRNA synthetase reveals an induced-fit ligand-recognition mechanism.,Wang W, Qin B, Wojdyla JA, Wang M, Gao X, Cui S IUCrJ. 2018 Jun 22;5(Pt 4):478-490. doi: 10.1107/S2052252518008217. eCollection, 2018 Jul 1. PMID:30002848<ref>PMID:30002848</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 5xgq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Ra]]
[[Category: Cui S]]
[[Category: Wang M]]
[[Category: Wang W]]
[[Category: Wojdyla JA]]