3whn: Difference between revisions
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==Hemerythrin-like domain of DcrH I119H mutant (met)== | |||
<StructureSection load='3whn' size='340' side='right' caption='[[3whn]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3whn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Desvh Desvh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WHN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WHN FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CFO:CHLORO+DIIRON-OXO+MOIETY'>CFO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3agt|3agt]], [[3agu|3agu]], [[3waq|3waq]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dcrH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=882 DESVH])</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=3whn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3whn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3whn RCSB], [http://www.ebi.ac.uk/pdbsum/3whn PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The O2-binding carboxylate-bridged diiron site in DcrH-Hr was engineered in an effort to perform the H2O2-dependent oxidation of external substrates. A His residue was introduced near the diiron site in place of a conserved residue, Ile119. The I119H variant promotes the oxidation of guaiacol and 1,4-cyclohexadiene upon addition of H2O2. | |||
HO-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin.,Okamoto Y, Onoda A, Sugimoto H, Takano Y, Hirota S, Kurtz DM, Shiro Y, Hayashi T Chem Commun (Camb). 2014 Jan 8. PMID:24400317<ref>PMID:24400317</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Hayashi, T | == References == | ||
[[Category: Hirota, S | <references/> | ||
[[Category: Kurtz, D M | __TOC__ | ||
[[Category: Okamoto, Y | </StructureSection> | ||
[[Category: Onoda, A | [[Category: Desvh]] | ||
[[Category: Shiro, Y | [[Category: Hayashi, T]] | ||
[[Category: Sugimoto, H | [[Category: Hirota, S]] | ||
[[Category: Takano, Y | [[Category: Kurtz, D M]] | ||
[[Category: Okamoto, Y]] | |||
[[Category: Onoda, A]] | |||
[[Category: Shiro, Y]] | |||
[[Category: Sugimoto, H]] | |||
[[Category: Takano, Y]] | |||
[[Category: Helix bundle]] | [[Category: Helix bundle]] | ||
[[Category: Metal binding protein]] | [[Category: Metal binding protein]] | ||
[[Category: Metal-binding]] | [[Category: Metal-binding]] | ||
[[Category: Oxygen sensor]] | [[Category: Oxygen sensor]] | ||
