4me4: Difference between revisions

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'''Unreleased structure'''


The entry 4me4 is ON HOLD
==Crystal structure of a HD-GYP domain (a cyclic-di-GMP phosphodiesterase) containing a tri-nuclear metal centre==
<StructureSection load='4me4' size='340' side='right'caption='[[4me4]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4me4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Persephonella_marina_EX-H1 Persephonella marina EX-H1]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4ME4 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]] 2.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4me4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4me4 OCA], [https://pdbe.org/4me4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4me4 RCSB], [https://www.ebi.ac.uk/pdbsum/4me4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4me4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C0QQ26_PERMH C0QQ26_PERMH]
<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.


Authors: Bellini, D., Walsh, M.A., Oxford Protein Production Facility (OPPF)
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>


Description: Metallo-enzyme from P. marina
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4me4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Persephonella marina EX-H1]]
[[Category: Bellini D]]
[[Category: Walsh MA]]
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