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==(R)-2-hydroxyisocaproyl-CoA dehydratase in complex with its substrate (R)-2-hydroxyisocaproyl-CoA==
==(R)-2-hydroxyisocaproyl-CoA dehydratase in complex with its substrate (R)-2-hydroxyisocaproyl-CoA==
<StructureSection load='3o3n' size='340' side='right' caption='[[3o3n]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3o3n' size='340' side='right'caption='[[3o3n]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3o3n]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_difficilis"_hall_and_o'toole_1935 "bacillus difficilis" hall and o'toole 1935]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O3N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O3N FirstGlance]. <br>
<table><tr><td colspan='2'>[[3o3n]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile Clostridioides difficile]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O3N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O3N FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=IRC:S-[2-[3-[[(2R)-4-[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-4-hydroxy-3-phosphonooxy-oxolan-2-yl]methoxy-hydroxy-phosphoryl]oxy-hydroxy-phosphoryl]oxy-2-hydroxy-3,3-dimethyl-butanoyl]amino]propanoylamino]ethyl]+(2R)-2-hydroxy-4-methyl-pentanethioate'>IRC</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o3m|3o3m]], [[3o3o|3o3o]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=H2S:HYDROSULFURIC+ACID'>H2S</scene>, <scene name='pdbligand=IRC:S-{(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl}+(2R)-2-hydroxy-4-methylpentanethioate+(non-preferred+name)'>IRC</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hadB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935]), hadC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1496 "Bacillus difficilis" Hall and O'Toole 1935])</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=3o3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o3n OCA], [https://pdbe.org/3o3n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o3n RCSB], [https://www.ebi.ac.uk/pdbsum/3o3n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o3n ProSAT]</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=3o3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o3n OCA], [http://pdbe.org/3o3n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o3n RCSB], [http://www.ebi.ac.uk/pdbsum/3o3n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o3n ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HADB_CLODI HADB_CLODI] Involved in the reductive branch of L-leucine fermentation. Catalyzes the irreversible beta/alpha-elimination of water from (R)-2-hydroxyisocaproyl-CoA to yield isocaprenoyl-CoA. This beta/alpha-dehydration depends on the reductive formation of ketyl radicals on the substrate generated by injection of a single electron from the ATP-dependent activator protein HadI. The enzyme is specific for the R-isomer.<ref>PMID:15654892</ref> <ref>PMID:21366233</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus difficilis hall and o'toole 1935]]
[[Category: Clostridioides difficile]]
[[Category: Buckel, W]]
[[Category: Large Structures]]
[[Category: Dobbek, H]]
[[Category: Buckel W]]
[[Category: Knauer, S H]]
[[Category: Dobbek H]]
[[Category: Atypical dehydratase]]
[[Category: Knauer SH]]
[[Category: Lyase]]
Retrieved from "https://proteopedia.org/3o3n"