View source for 2yq4


==Crystal Structure of D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus==
<StructureSection load='2yq4' size='340' side='right'caption='[[2yq4]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2yq4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_delbrueckii_subsp._bulgaricus Lactobacillus delbrueckii subsp. bulgaricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YQ4 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]] 3.45&#8491;</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=2yq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yq4 OCA], [https://pdbe.org/2yq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yq4 RCSB], [https://www.ebi.ac.uk/pdbsum/2yq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yq4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q1GAA2_LACDA Q1GAA2_LACDA] 
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== Publication Abstract from PubMed ==
Hydroxyacid dehydrogenases, responsible for the stereospecific conversion of 2-keto acids to 2-hydroxyacids in lactic acid producing bacteria, have a range of biotechnology applications including antibiotic synthesis, flavor development in dairy products and the production of valuable synthons. The genome of Lactobacillus delbrueckii ssp. bulgaricus, a member of the heterogeneous group of lactic acid bacteria, encodes multiple hydroxyacid dehydrogenases whose structural and functional properties remain poorly characterized. Here, we report the apo and coenzyme NAD(+) complexed crystal structures of the L. bulgaricusD-isomer specific 2-hydroxyacid dehydrogenase, D2-HDH. Comparison with closely related members of the NAD-dependent dehydrogenase family reveals that whilst the D2-HDH core fold is structurally conserved, the substrate-binding site has a number of non-canonical features that may influence substrate selection and thus dictate the physiological function of the enzyme.

Structural characterization of a D-isomer specific 2-hydroxyacid dehydrogenase from Lactobacillus delbrueckii ssp. bulgaricus.,Holton SJ, Anandhakrishnan M, Geerlof A, Wilmanns M J Struct Biol. 2012 Oct 27. pii: S1047-8477(12)00291-2. doi:, 10.1016/j.jsb.2012.10.009. PMID:23110853<ref>PMID:23110853</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 2yq4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Lactobacillus delbrueckii subsp. bulgaricus]]
[[Category: Large Structures]]
[[Category: Anandhakrishnan M]]
[[Category: Geerlof A]]
[[Category: Holton SJ]]
[[Category: Wilmanns M]]