4ly4: Difference between revisions
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==Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori== | |||
<StructureSection load='4ly4' size='340' side='right' caption='[[4ly4]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ly4]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Helpg Helpg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LY4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LY4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP0310, HPG27_289 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=563041 HELPG])</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=4ly4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ly4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ly4 RCSB], [http://www.ebi.ac.uk/pdbsum/4ly4 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Peptidoglycan deacetlyase (HP0310, HpPgdA) from the gram-negative pathogen Helicobacter pylori, is the enzyme responsible for a peptidoglycan modification that counteracts the host immune response. In a recent study, we determined the crystallographic structure of the enzyme, which is a homo-tetramer (Shaik et al., PloS One 2011;6:e19207). The metal-binding site, which is essential for the enzyme's catalytic activity, is visible within the structure, but we were unable to identify the nature of the metal itself. In this study, we have obtained a higher-resolution crystal structure of the enzyme, which shows that the ion bound is, in fact, zinc. Analysis of the structure of the four sites, one per monomer, and quantum chemical calculations of models of the site in the presence of different divalent metal ions show an intrinsic preference for zinc, but also significant flexibility of the site so that binding of other ions can eventually occur. Proteins 2014. (c) 2013 Wiley Periodicals, Inc. | |||
Characterization of the divalent metal binding site of bacterial polysaccharide deacetylase using crystallography and quantum chemical calculations.,Munan Shaik M, Bhattacharjee N, Bhattacharjee A, Field MJ, Zanotti G Proteins. 2013 Dec 17. doi: 10.1002/prot.24497. PMID:24346839<ref>PMID:24346839</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Helpg]] | [[Category: Helpg]] | ||
[[Category: Shaik, M M.]] | [[Category: Shaik, M M.]] | ||
Revision as of 08:26, 8 October 2014
Crystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pyloriCrystal structure of peptidoglycan deacetylase (HP0310) with Zinc from Helicobacter pylori
Structural highlights
Publication Abstract from PubMedPeptidoglycan deacetlyase (HP0310, HpPgdA) from the gram-negative pathogen Helicobacter pylori, is the enzyme responsible for a peptidoglycan modification that counteracts the host immune response. In a recent study, we determined the crystallographic structure of the enzyme, which is a homo-tetramer (Shaik et al., PloS One 2011;6:e19207). The metal-binding site, which is essential for the enzyme's catalytic activity, is visible within the structure, but we were unable to identify the nature of the metal itself. In this study, we have obtained a higher-resolution crystal structure of the enzyme, which shows that the ion bound is, in fact, zinc. Analysis of the structure of the four sites, one per monomer, and quantum chemical calculations of models of the site in the presence of different divalent metal ions show an intrinsic preference for zinc, but also significant flexibility of the site so that binding of other ions can eventually occur. Proteins 2014. (c) 2013 Wiley Periodicals, Inc. Characterization of the divalent metal binding site of bacterial polysaccharide deacetylase using crystallography and quantum chemical calculations.,Munan Shaik M, Bhattacharjee N, Bhattacharjee A, Field MJ, Zanotti G Proteins. 2013 Dec 17. doi: 10.1002/prot.24497. PMID:24346839[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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