1k2w: Difference between revisions
No edit summary |
No edit summary |
||
Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1k2w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter 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 [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 [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K2W FirstGlance]. <br> | ||
</td></tr><tr><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='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> | ||
<tr><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://www.rcsb.org/pdb/explore.do?structureId=1k2w RCSB], [http://www.ebi.ac.uk/pdbsum/1k2w PDBsum]</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=1k2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k2w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k2w RCSB], [http://www.ebi.ac.uk/pdbsum/1k2w PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 30: | Line 32: | ||
[[Category: L-iditol 2-dehydrogenase]] | [[Category: L-iditol 2-dehydrogenase]] | ||
[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
[[Category: Philippsen, A | [[Category: Philippsen, A]] | ||
[[Category: Schirmer, T | [[Category: Schirmer, T]] | ||
[[Category: Stetefeld, J | [[Category: Stetefeld, J]] | ||
[[Category: Enzyme]] | [[Category: Enzyme]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Short-chain dehydrogenase]] | [[Category: Short-chain dehydrogenase]] |
Revision as of 16:40, 25 December 2014
Crystal structure of sorbitol dehydrogenase from R. sphaeroidesCrystal structure of sorbitol dehydrogenase from R. sphaeroides
Structural highlights
Function[DHSO_RHOSH] Catalyzes the oxidation of D-glucitol (sorbitol) to D-fructose, galactitol to D-tagatose and of L-iditol. 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 PubMedRecombinant 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|