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4mdz

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{{STRUCTURE_4mdz| PDB=4mdz | SCENE= }}
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==Metallo-enzyme from P. marina==
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===Metallo-enzyme from P. marina===
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<StructureSection load='4mdz' size='340' side='right' caption='[[4mdz]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
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{{ABSTRACT_PUBMED_24176013}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4mdz]] 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=4MDZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MDZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3AS,5S,7AR,9R,10R,10AS,12S,14AR)-3,5,10,12-TETRAHYDROXY-5,12-DIOXIDOOCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-2,9-DIYL]BIS(2-AMINO-1,9-DIHYDRO-6H-PURIN-6-ONE)'>C2E</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mcw|4mcw]], [[4me4|4me4]]</td></tr>
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<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>
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<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=4mdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mdz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mdz RCSB], [http://www.ebi.ac.uk/pdbsum/4mdz PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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[[4mdz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MDZ OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:024176013</ref><references group="xtra"/><references/>
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</div>
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[[Category: Bellini, D.]]
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== References ==
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[[Category: OPPF, Oxford Protein Production Facility.]]
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<references/>
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[[Category: Walsh, M A.]]
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__TOC__
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</StructureSection>
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[[Category: Permh]]
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[[Category: Bellini, D]]
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[[Category: OPPF, Oxford Protein Production Facility]]
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[[Category: Walsh, M A]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Oppf]]
[[Category: Oppf]]

Revision as of 09:04, 5 January 2015

Metallo-enzyme from P. marina

4mdz, resolution 2.68Å

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