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| | ==Crystal structure of sorbitol dehydrogenase from R. sphaeroides== | | ==Crystal structure of sorbitol dehydrogenase from R. sphaeroides== |
| - | <StructureSection load='1k2w' size='340' side='right' caption='[[1k2w]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='1k2w' size='340' side='right'caption='[[1k2w]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1k2w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K2W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K2W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1k2w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1K2W FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-iditol_2-dehydrogenase L-iditol 2-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.14 1.1.1.14] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</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=1k2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k2w OCA], [http://pdbe.org/1k2w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1k2w RCSB], [http://www.ebi.ac.uk/pdbsum/1k2w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1k2w ProSAT]</span></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=1k2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k2w OCA], [https://pdbe.org/1k2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1k2w RCSB], [https://www.ebi.ac.uk/pdbsum/1k2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1k2w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DHSO_RHOSH DHSO_RHOSH]] Catalyzes the oxidation of D-glucitol (sorbitol) to D-fructose, galactitol to D-tagatose and of L-iditol. | + | [https://www.uniprot.org/uniprot/SDH_CERSP SDH_CERSP] Catalyzes the oxidation of D-sorbitol (D-glucitol) to D-fructose. Can also catalyze the oxidation of galactitol to D-tagatose and the oxidation of L-iditol, with lower efficiency.<ref>PMID:7551049</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Rhodococcus capsulatus molisch 1907]] | + | [[Category: Cereibacter sphaeroides]] |
| - | [[Category: L-iditol 2-dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Philippsen, A]] | + | [[Category: Philippsen A]] |
| - | [[Category: Schirmer, T]] | + | [[Category: Schirmer T]] |
| - | [[Category: Stetefeld, J]] | + | [[Category: Stetefeld J]] |
| - | [[Category: Enzyme]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Short-chain dehydrogenase]]
| + | |
| Structural highlights
Function
SDH_CERSP Catalyzes the oxidation of D-sorbitol (D-glucitol) to D-fructose. Can also catalyze the oxidation of galactitol to D-tagatose and the oxidation of L-iditol, with lower efficiency.[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
Recombinant sorbitol dehydrogenase (SDH) from Rhodobacter sphaeroides has been crystallized in the absence of the cofactor NAD(H) and its structure determined to 2.4 A resolution using molecular replacement (refined R and R free factors of 18.8 and 23.8%, respectively). As expected from the sequence and shown by the conserved fold, SDH can be assigned to the short-chain dehydrogenase/reductase protein family. The cofactor NAD and the substrate sorbitol have been modelled into the structure and the active-site architecture, which displays the highly conserved catalytic tetrad of Asn-Ser-Tyr-Lys residues, is discussed in relation to the enzyme mechanism. This is the first structure of a bacterial SDH belonging to the SDR family.
Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 A resolution.,Philippsen A, Schirmer T, Stein MA, Giffhorn F, Stetefeld J Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):374-9. Epub 2005, Mar 24. PMID:15805591[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schauder S, Schneider KH, Giffhorn F. Polyol metabolism of Rhodobacter sphaeroides: biochemical characterization of a short-chain sorbitol dehydrogenase. Microbiology (Reading). 1995 Aug;141 ( Pt 8):1857-1863. PMID:7551049 doi:10.1099/13500872-141-8-1857
- ↑ Philippsen A, Schirmer T, Stein MA, Giffhorn F, Stetefeld J. Structure of zinc-independent sorbitol dehydrogenase from Rhodobacter sphaeroides at 2.4 A resolution. Acta Crystallogr D Biol Crystallogr. 2005 Apr;61(Pt 4):374-9. Epub 2005, Mar 24. PMID:15805591 doi:10.1107/S0907444904034390
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