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3a28

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Revision as of 12:15, 29 July 2020

Crystal structure of L-2,3-butanediol dehydrogenase

Structural highlights

3a28 is a 8 chain structure with sequence from "micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1geg
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BUDC_CORGT] Catalyzes the reversible reduction of (S)-acetoin to (S,S)-butane-2,3-diol (L-BD) in the presence of NADH. To a lesser extent, can also catalyze the irreversible reduction of diacetyl to (S)-acetoin. Cannot oxidize meso-BD, D-BD, 2-butanol, 1,2-propanediol, ethanol, acetol, 1,2-butanediol, 1,3-butanediol, n-butanol, and n-propanol. Cannot reduce (R)-acetoin, acetol, dihydroxyacetone and 2,4-pentanedione.[REFERENCE:1]^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

2,3-butanediol dehydrogenase (BDH) catalyzes the NAD-dependent redox reaction between acetoin and 2,3-butanediol. There are three types of homologous BDH, each stereospecific for both substrate and product. To establish how these homologous enzymes possess differential stereospecificities, we determined the crystal structure of l-BDH with a bound inhibitor at 2.0 A. Comparison with the inhibitor binding mode of meso-BDH highlights the role of a hydrogen-bond from a conserved Trp residue(192). Site-directed mutagenesis of three active site residues of meso-BDH, including Trp(190), which corresponds to Trp(192) of L-BDH, converted its stereospecificity to that of L-BDH. This result confirms the importance of conserved residues in modifying the stereospecificity of homologous enzymes.

Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases.,Otagiri M, Ui S, Takusagawa Y, Ohtsuki T, Kurisu G, Kusunoki M FEBS Lett. 2010 Jan 4;584(1):219-23. Epub . PMID:19941855^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Takusagawa Y, Otagiri M, Ui S, Ohtsuki T, Mimura A, Ohkuma M, Kudo T. Purification and characterization of L-2,3-butanediol dehydrogenase of Brevibacterium saccharolyticum C-1012 expressed in Escherichia coli. Biosci Biotechnol Biochem. 2001 Aug;65(8):1876-8. PMID:11577733
↑ Otagiri M, Ui S, Takusagawa Y, Ohtsuki T, Kurisu G, Kusunoki M. Structural basis for chiral substrate recognition by two 2,3-butanediol dehydrogenases. FEBS Lett. 2010 Jan 4;584(1):219-23. Epub . PMID:19941855 doi:10.1016/j.febslet.2009.11.068

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3a28"

@@ Line 1: / Line 1: @@
 ==Crystal structure of L-2,3-butanediol dehydrogenase==
-<StructureSection load='3a28' size='340' side='right' caption='[[3a28]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3a28' size='340' side='right'caption='[[3a28]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3a28]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A28 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A28 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3a28]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_glutamicus"_kinoshita_et_al._1958 "micrococcus glutamicus" kinoshita et al. 1958]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A28 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3A28 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1geg|1geg]]</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=3a28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a28 OCA], [http://pdbe.org/3a28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a28 RCSB], [http://www.ebi.ac.uk/pdbsum/3a28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a28 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3a28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a28 OCA], [http://pdbe.org/3a28 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a28 RCSB], [http://www.ebi.ac.uk/pdbsum/3a28 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a28 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 34: / Line 34: @@
 </StructureSection>
 [[Category: Micrococcus glutamicus kinoshita et al. 1958]]
+[[Category: Large Structures]]
 [[Category: Kurisu, G]]
 [[Category: Kusunoki, M]]

3a28

From Proteopedia

Revision as of 12:15, 29 July 2020

Crystal structure of L-2,3-butanediol dehydrogenase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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