4c3o
From Proteopedia
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| - | + | ==Structure and function of an oxygen tolerant NiFe hydrogenase from Salmonella== | |
| - | + | <StructureSection load='4c3o' size='340' side='right' caption='[[4c3o]], [[Resolution|resolution]] 3.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4c3o]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C3O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C3O FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=F4S:FE4-S3+CLUSTER'>F4S</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NFU:FORMYL[BIS(HYDROCYANATO-1KAPPAC)]IRONNICKEL(FE-NI)'>NFU</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferredoxin_hydrogenase Ferredoxin hydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.12.7.2 1.12.7.2] </span></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=4c3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c3o RCSB], [http://www.ebi.ac.uk/pdbsum/4c3o PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Salmonella enterica is an opportunistic pathogen that produces a [NiFe]-hydrogenase under aerobic conditions. Here, genetic engineering approaches were used to facilitate isolation of this enzyme, termed Hyd-5. The crystal structure was determined to a resolution of 3.2 A and the hydrogenase was observed to comprise associated large and small subunits. The structure indicated that residue H229 from the large subunit was close to the proximal [4Fe-3S] cluster in the small subunit. In addition, H229 was observed to lie close to a buried glutamic acid (E73), which is conserved in oxygen-tolerant hydrogenases. Residues H229 and E73 of the Hyd-5 large subunit were found to be important in both hydrogen oxidation activity and the oxygen tolerance mechanism. Substitution of H229 or E73 with alanine led to a loss in the ability of Hyd-5 to oxidise hydrogen in air. Furthermore, the H229A variant was found to have lost the overpotential requirement for activity that is always observed with oxygen-tolerant [NiFe]-hydrogenases. It is possible that H229 has a role in stabilising the super-oxidised form of the proximal cluster in the presence of oxygen, and it is proposed that E73 could play a supporting role in fine-tuning the chemistry of H229 to enable this function. | ||
| - | + | How the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenase.,Bowman L, Flanagan L, Fyfe PK, Parkin A, Hunter WN, Sargent F Biochem J. 2014 Jan 16. PMID:24428762<ref>PMID:24428762</ref> | |
| - | [ | + | |
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ferredoxin hydrogenase]] | [[Category: Ferredoxin hydrogenase]] | ||
| - | [[Category: Bowman, L | + | [[Category: Salty]] |
| - | [[Category: Flanagan, L | + | [[Category: Bowman, L]] |
| - | [[Category: Fyfe, P K | + | [[Category: Flanagan, L]] |
| - | [[Category: Hunter, W N | + | [[Category: Fyfe, P K]] |
| - | [[Category: Parkin, A | + | [[Category: Hunter, W N]] |
| - | [[Category: Sargent, F | + | [[Category: Parkin, A]] |
| + | [[Category: Sargent, F]] | ||
[[Category: Hydrogen metabolism]] | [[Category: Hydrogen metabolism]] | ||
[[Category: Nife hydrogenase]] | [[Category: Nife hydrogenase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 16:27, 21 December 2014
Structure and function of an oxygen tolerant NiFe hydrogenase from Salmonella
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