4n5l
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase from Ralstonia eutropha== | |
| + | <StructureSection load='4n5l' size='340' side='right'caption='[[4n5l]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4n5l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cupriavidus_necator_H16 Cupriavidus necator H16]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N5L 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]] 1.65Å</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=4n5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n5l OCA], [https://pdbe.org/4n5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n5l RCSB], [https://www.ebi.ac.uk/pdbsum/4n5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n5l ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PHAB_CUPNH PHAB_CUPNH] Catalyzes the chiral reduction of acetoacetyl-CoA to (R)-3-hydroxybutyryl-CoA. Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation.<ref>PMID:23913421</ref> <ref>PMID:24211201</ref> <ref>PMID:2670935</ref> <ref>PMID:2670936</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | (R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from Ralstonia eutropha H16 (RePhaB) is an enzyme that catalyzes the NADPH-dependent reduction of acetoacetyl-CoA, an intermediate of polyhydroxyalkanoates (PHA) synthetic pathways. Polymeric PHA is used to make bioplastics, implant biomaterials, and biofuels. Here, we report the crystal structures of RePhaB apoenzyme and in complex with either NADP+ or acetoacetyl-CoA, which provide the catalytic mechanism of the protein. RePhaB contains a Rossmann fold and a Clamp domain for binding of NADP+ and acetoacetyl-CoA, respectively. The NADP+-bound form of RePhaB structure reveals that the protein has a unique cofactor binding mode. Interestingly, in the RePhaB structure in complex with acetoacetyl-CoA, the conformation of the Clamp domain, especially the Clamp-lid, undergoes a large structural change about 4.6A leading to formation of the substrate pocket. These structural observations, along with the biochemical experiments, suggest that movement of the Clamp-lid enables the substrate binding and ensures the acetoacetyl moiety is located near to the nicotinamide ring of NADP+. | ||
| - | + | Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase PhaB from Ralstonia eutropha.,Kim J, Chang JH, Kim EJ, Kim KJ Biochem Biophys Res Commun. 2013 Nov 6. pii: S0006-291X(13)01843-3. doi:, 10.1016/j.bbrc.2013.10.150. PMID:24211201<ref>PMID:24211201</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4n5l" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Cupriavidus necator H16]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kim J-E]] | ||
| + | [[Category: Kim K-J]] | ||
| + | [[Category: Kim S]] | ||
Current revision
Crystal structure of (R)-3-hydroxybutyryl-CoA dehydrogenase from Ralstonia eutropha
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