View source for 5lu7


==Heptose isomerase GmhA mutant - D61A==
<StructureSection load='5lu7' size='340' side='right'caption='[[5lu7]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lu7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei_K96243 Burkholderia pseudomallei K96243]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LU7 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]] 1.92&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=M7P:D-GLYCERO-D-MANNOPYRANOSE-7-PHOSPHATE'>M7P</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5lu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lu7 OCA], [https://pdbe.org/5lu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lu7 RCSB], [https://www.ebi.ac.uk/pdbsum/5lu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lu7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GMHA_BURPS GMHA_BURPS] Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.<ref>PMID:20447408</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cooperativity is a feature many multimeric proteins use to control activity. Here we show that the bacterial heptose isomerase GmhA displays homotropic positive and negative cooperativity among its four protomers. Most similar proteins achieve this through conformational changes: GmhA instead employs a delicate network of hydrogen bonds, and couples pairs of active sites controlled by a unique water channel. This network apparently raises the Lewis acidity of the catalytic zinc, thus increasing the activity at one active site at the cost of preventing substrate from adopting a reactive conformation at the paired negatively cooperative site - a "half-site" behavior. Our study establishes the principle that multimeric enzymes can exploit this cooperativity without conformational changes to maximize their catalytic power and control. More broadly, this subtlety by which enzymes regulate functions could be used to explore new inhibitor design strategies.

A half-site multimeric enzyme achieves its cooperativity without conformational changes.,Vivoli M, Pang J, Harmer NJ Sci Rep. 2017 Nov 28;7(1):16529. doi: 10.1038/s41598-017-16421-2. PMID:29184087<ref>PMID:29184087</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lu7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Burkholderia pseudomallei K96243]]
[[Category: Large Structures]]
[[Category: Harmer NJ]]
[[Category: Pang J]]
[[Category: Vivoli M]]