4me4
From Proteopedia
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| - | + | ==Metallo-enzyme from P. marina== | |
| - | === | + | <StructureSection load='4me4' size='340' side='right' caption='[[4me4]], [[Resolution|resolution]] 2.55Å' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4me4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Permh Permh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ME4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ME4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mcw|4mcw]], [[4mdz|4mdz]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PERMA_0986 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=123214 PERMH])</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=4me4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4me4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4me4 RCSB], [http://www.ebi.ac.uk/pdbsum/4me4 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bis-(3',5') cyclic di-guanylate (c-di-GMP) is a key bacterial second messenger that is implicated in the regulation of many crucial processes that include biofilm formation, motility and virulence. Cellular levels of c-di-GMP are controlled through synthesis by GGDEF domain diguanylate cyclases and degradation by two classes of phosphodiesterase with EAL or HD-GYP domains. Here, we have determined the structure of an enzymatically active HD-GYP domain protein from Persephonella marina (PmGH) alone, in complex with substrate (c-di-GMP) and final reaction product (GMP). The structures reveal a novel trinuclear iron binding site, which is implicated in catalysis and identify residues involved in recognition of c-di-GMP. This structure completes the picture of all domains involved in c-di-GMP metabolism and reveals that the HD-GYP family splits into two distinct subgroups containing bi- and trinuclear metal centres. | ||
| - | + | Crystal structure of an HD-GYP domain cyclic-di-GMP phosphodiesterase reveals an enzyme with a novel trinuclear catalytic iron centre.,Bellini D, Caly DL, McCarthy Y, Bumann M, An SQ, Dow JM, Ryan RP, Walsh MA Mol Microbiol. 2014 Jan;91(1):26-38. doi: 10.1111/mmi.12447. Epub 2013 Nov 24. PMID:24176013<ref>PMID:24176013</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Bellini, D | + | == References == |
| - | [[Category: OPPF, Oxford Protein Production Facility | + | <references/> |
| - | [[Category: Walsh, M A | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Permh]] | ||
| + | [[Category: Bellini, D]] | ||
| + | [[Category: OPPF, Oxford Protein Production Facility]] | ||
| + | [[Category: Walsh, M A]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Oppf]] | [[Category: Oppf]] | ||
Revision as of 09:36, 5 January 2015
Metallo-enzyme from P. marina
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