View source for 5je8


==The crystal structure of Bacillus cereus 3-hydroxyisobutyrate dehydrogenase in complex with NAD==
<StructureSection load='5je8' size='340' side='right'caption='[[5je8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5je8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5JE8 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5je8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5je8 OCA], [https://pdbe.org/5je8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5je8 RCSB], [https://www.ebi.ac.uk/pdbsum/5je8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5je8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q81DR6_BACCR Q81DR6_BACCR] 
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5je8" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus cereus ATCC 14579]]
[[Category: Large Structures]]
[[Category: Park SC]]
[[Category: Yoon SI]]