7yh5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==MazG(Mycobacterium tuberculosis)== | |
| + | <StructureSection load='7yh5' size='340' side='right'caption='[[7yh5]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7yh5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YH5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YH5 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]] 2.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7yh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7yh5 OCA], [https://pdbe.org/7yh5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7yh5 RCSB], [https://www.ebi.ac.uk/pdbsum/7yh5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7yh5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A0E7YXB3_MYCTX A0A0E7YXB3_MYCTX] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The housecleaning enzyme of Mycobacterium tuberculosis (Mtb), MazG, is a nucleoside triphosphate pyrophosphohydrolase (NTP-PPase) and can hydrolyze all canonical or non-canonical NTPs into NMPs and pyrophosphate. The Mycobacterium tuberculosis MazG (Mtb-MazG) contributes to antibiotic resistance in response to oxidative or nitrosative stress under dormancy, making it a promising target for treating TB in latent infection patients. However, the structural basis of Mtb-MazG is not clear. Here we describe the crystal structure of Mtb-MazG (1-185) at 2.7 A resolution, composed of two similar folded spherical domains in tandem. Unlike other all-alpha NTP pyrophosphatases, Mtb-MazG has an N-terminal extra region composed of three alpha-helices and five beta-strands. The second domain is global, with five alpha-helices located in the N-terminal domain. Gel-filtration assay and SAXS analysis show that Mtb-MazG forms an enzyme-active dimer in solution. In addition, the metal ion Mg(2+) is bound with four negative-charged residues Glu119, Glu122, Glu138, and Asp141. Different truncations and site-directed mutagenesis revealed that the full-length dimeric form and the metal ion Mg(2+) are indispensable for the catalytic activity of Mtb-MazG. Thus, our work provides new insights into understanding the molecular basis of Mtb-MazG. | ||
| - | + | Structural analysis of the housecleaning nucleoside triphosphate pyrophosphohydrolase MazG from Mycobacterium tuberculosis.,Wang S, Gao B, Chen A, Zhang Z, Wang S, Lv L, Zhao G, Li J Front Microbiol. 2023 Mar 1;14:1137279. doi: 10.3389/fmicb.2023.1137279. , eCollection 2023. PMID:36937295<ref>PMID:36937295</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Li | + | <div class="pdbe-citations 7yh5" style="background-color:#fffaf0;"></div> |
| - | [[Category: Wang | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycobacterium tuberculosis]] | ||
| + | [[Category: Li J]] | ||
| + | [[Category: Wang S]] | ||
Revision as of 06:09, 19 July 2023
MazG(Mycobacterium tuberculosis)
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