5xgq: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 5xgq~~ is ~~ON HOLD~~

==Crystal structure of apo form (free-state) Mycobacterium tuberculosis methionyl-tRNA synthetase==

== 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]] 1.899Å</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]

== 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.

~~Authors:~~ Wang, W., Wang, M., ~~Wojdyla~~, J.A., ~~Cui, S~~.

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>

~~Description~~: ~~aminoacyl-~~tRNA synthetase ~~from Bacterium~~

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

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: ~~Wang, M~~]]

[[Category: Wang~~, W~~]]

[[Category: ~~Wojdyla, J.A~~]]

==See Also==

[[Category: ~~Cui, S~~]]

*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]

== References ==

__TOC__

</StructureSection>

[[Category: Large Structures]]

[[Category: Mycobacterium tuberculosis H37Ra]]

[[Category: Cui S]]

[[Category: Wang M]]

[[Category: Wang W]]

[[Category: Wojdyla JA]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5xgq is ON HOLD
+==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]
+<div style="background-color:#fffaf0;">
+== 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.
-Authors: Wang, W., Wang, M., Wojdyla, J.A., Cui, S.
+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>
-Description: aminoacyl-tRNA synthetase from Bacterium
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Wang, M]]
+<div class="pdbe-citations 5xgq" style="background-color:#fffaf0;"></div>
-[[Category: Wang, W]]
-[[Category: Wojdyla, J.A]]
+==See Also==
-[[Category: Cui, S]]
+*[[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]]