4lq6: Difference between revisions
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==Crystal structure of Rv3717 reveals a novel amidase from M. tuberculosis== | |||
<StructureSection load='4lq6' size='340' side='right'caption='[[4lq6]], [[Resolution|resolution]] 1.68Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4lq6]] is a 1 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=4LQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LQ6 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]] 1.68Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4lq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lq6 OCA], [https://pdbe.org/4lq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lq6 RCSB], [https://www.ebi.ac.uk/pdbsum/4lq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lq6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O69684_MYCTO O69684_MYCTO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial N-acetylmuramoyl-L-alanine amidases are cell-wall hydrolases that hydrolyze the bond between N-acetylmuramic acid and L-alanine in cell-wall glycopeptides. Rv3717 of Mycobacterium tuberculosis has been identified as a unique autolysin that lacks a cell-wall-binding domain (CBD) and its structure has been determined to 1.7 A resolution by the Pt-SAD phasing method. Rv3717 possesses an alpha/beta-fold and is a zinc-dependent hydrolase. The structure reveals a short flexible hairpin turn that partially occludes the active site and may be involved in autoregulation. This type of autoregulation of activity of PG hydrolases has been observed in Bartonella henselae amidase (AmiB) and may be a general mechanism used by some of the redundant amidases to regulate cell-wall hydrolase activity in bacteria. Rv3717 utilizes its net positive charge for substrate binding and exhibits activity towards a broad spectrum of substrate cell walls. The enzymatic activity of Rv3717 was confirmed by isolation and identification of its enzymatic products by LC/MS. These studies indicate that Rv3717, an N-acetylmuramoyl-L-alanine amidase from M. tuberculosis, represents a new family of lytic amidases that do not have a separate CBD and are regulated conformationally. | |||
The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis.,Kumar A, Kumar S, Kumar D, Mishra A, Dewangan RP, Shrivastava P, Ramachandran S, Taneja B Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2543-54. doi:, 10.1107/S0907444913026371. Epub 2013 Nov 19. PMID:24311595<ref>PMID:24311595</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4lq6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mycobacterium tuberculosis]] | |||
[[Category: Dewangan RP]] | |||
[[Category: Kumar A]] | |||
[[Category: Kumar D]] | |||
[[Category: Kumar S]] | |||
[[Category: Mishra A]] | |||
[[Category: Ramachandran S]] | |||
[[Category: Shrivastava P]] | |||
[[Category: Taneja B]] | |||
Latest revision as of 14:06, 6 November 2024
Crystal structure of Rv3717 reveals a novel amidase from M. tuberculosisCrystal structure of Rv3717 reveals a novel amidase from M. tuberculosis
Structural highlights
FunctionPublication Abstract from PubMedBacterial N-acetylmuramoyl-L-alanine amidases are cell-wall hydrolases that hydrolyze the bond between N-acetylmuramic acid and L-alanine in cell-wall glycopeptides. Rv3717 of Mycobacterium tuberculosis has been identified as a unique autolysin that lacks a cell-wall-binding domain (CBD) and its structure has been determined to 1.7 A resolution by the Pt-SAD phasing method. Rv3717 possesses an alpha/beta-fold and is a zinc-dependent hydrolase. The structure reveals a short flexible hairpin turn that partially occludes the active site and may be involved in autoregulation. This type of autoregulation of activity of PG hydrolases has been observed in Bartonella henselae amidase (AmiB) and may be a general mechanism used by some of the redundant amidases to regulate cell-wall hydrolase activity in bacteria. Rv3717 utilizes its net positive charge for substrate binding and exhibits activity towards a broad spectrum of substrate cell walls. The enzymatic activity of Rv3717 was confirmed by isolation and identification of its enzymatic products by LC/MS. These studies indicate that Rv3717, an N-acetylmuramoyl-L-alanine amidase from M. tuberculosis, represents a new family of lytic amidases that do not have a separate CBD and are regulated conformationally. The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis.,Kumar A, Kumar S, Kumar D, Mishra A, Dewangan RP, Shrivastava P, Ramachandran S, Taneja B Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2543-54. doi:, 10.1107/S0907444913026371. Epub 2013 Nov 19. PMID:24311595[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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