5je8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The crystal structure of Bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD== |
| + | <StructureSection load='5je8' size='340' side='right' caption='[[5je8]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5je8]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JE8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JE8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-hydroxyisobutyrate_dehydrogenase 3-hydroxyisobutyrate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.31 1.1.1.31] </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=5je8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5je8 OCA], [http://pdbe.org/5je8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5je8 RCSB], [http://www.ebi.ac.uk/pdbsum/5je8 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 3-hydroxyisobutyrate dehydrogenase (HIBADH) family catalyzes the NAD+- or NADP+-dependent oxidation of various beta-hydroxyacid substrates into their cognate semialdehydes for diverse metabolic pathways. Because HIBADH group members exhibit different substrate specificities, the substrate-recognition mode of each enzyme should be individually characterized. In the current study, we report the biochemical and structural analysis of a HIBADH group enzyme from Bacillus cereus (bcHIBADH). bcHIBADH mediates a dehydrogenation reaction on S-3-hydroxyisobutyrate substrate with high catalytic efficiency in an NAD+-dependent manner; it also oxidizes l-serine and 3-hydroxypropionate with lower activity. bcHIBADH consists of two domains and is further assembled into a functional dimer rather than a tetramer that has been commonly observed in other prokaryotic HIBADH group members. In the bcHIBADH structure, the interdomain cleft forms a putative active site and simultaneously accommodates both an NAD+ cofactor and a substrate mimic. Our structure-based comparative analysis highlights structural motifs that are important in the cofactor and substrate recognition of the HIBADH group. | ||
| - | + | Structural and biochemical characterization of the Bacillus cereus 3-hydroxyisobutyrate dehydrogenase.,Park SC, Kim PH, Lee GS, Kang SG, Ko HJ, Yoon SI Biochem Biophys Res Commun. 2016 Apr 24. pii: S0006-291X(16)30640-4. doi:, 10.1016/j.bbrc.2016.04.126. PMID:27120461<ref>PMID:27120461</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Yoon, S | + | <div class="pdbe-citations 5je8" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: 3-hydroxyisobutyrate dehydrogenase]] | ||
| + | [[Category: Park, S C]] | ||
| + | [[Category: Yoon, S I]] | ||
| + | [[Category: Dehydrogenase]] | ||
| + | [[Category: Oxidoreductase]] | ||
Revision as of 16:55, 15 May 2016
The crystal structure of Bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD
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