4pmr
From Proteopedia
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| - | ''' | + | ==Crystal structure of the Mycobacterium tuberculosis Tat-secreted protein Rv2525c in complex with HEPES (monoclinic crystal form II)== |
| + | <StructureSection load='4pmr' size='340' side='right' caption='[[4pmr]], [[Resolution|resolution]] 1.81Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4pmr]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PMR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PMR FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=4pmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pmr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pmr RCSB], [http://www.ebi.ac.uk/pdbsum/4pmr PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Among the few proteins shown to be secreted by the Tat system in Mycobacterium tuberculosis, Rv2525c is of particular interest, since its gene is conserved in the minimal genome of Mycobacterium leprae. Previous evidence linked this protein to cell wall metabolism and sensitivity to beta-lactams. We describe here the crystal structure of Rv2525c that shows a TIM barrel-like fold characteristic of glycoside hydrolases of the GH25 family, which includes prokaryotic and phage-encoded peptidoglycan hydrolases. Structural comparison with other members of this family combined with substrate docking suggest that, although the 'neighbouring group' catalytic mechanism proposed for this family still appears as the most plausible, the identity of residues involved in catalysis in GH25 hydrolases might need to be revised. | ||
| - | + | Structural studies suggest a peptidoglycan hydrolase function for the Mycobacterium tuberculosis Tat-secreted protein Rv2525c.,Bellinzoni M, Haouz A, Miras I, Magnet S, Andre-Leroux G, Mukherjee R, Shepard W, Cole ST, Alzari PM J Struct Biol. 2014 Sep 24. pii: S1047-8477(14)00189-0. doi:, 10.1016/j.jsb.2014.09.003. PMID:25260828<ref>PMID:25260828</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Alzari, P M.]] | ||
| + | [[Category: Bellinzoni, M.]] | ||
| + | [[Category: Haouz, A.]] | ||
| + | [[Category: Shepard, W.]] | ||
| + | [[Category: Unknown function]] | ||
Revision as of 07:39, 8 October 2014
Crystal structure of the Mycobacterium tuberculosis Tat-secreted protein Rv2525c in complex with HEPES (monoclinic crystal form II)
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