3n2t

<StructureSection load='3n2t' size='340' side='right' caption='[[3n2t]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[3n2t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"acetobacter_capsulatum"_(sic)_shimwell_1936 "acetobacter capsulatum" (sic) shimwell 1936]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N2T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N2T FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GOX1615 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=442 "Acetobacter capsulatum" (sic) Shimwell 1936])</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=3n2t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n2t OCA], [http://pdbe.org/3n2t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n2t RCSB], [http://www.ebi.ac.uk/pdbsum/3n2t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n2t ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The NADP-dependent glycerol dehydrogenase (EC 1.1.1.72) from Gluconobacter oxydans is a member of family 11 of the aldo-keto reductase (AKR) enzyme superfamily; according to the systematic nomenclature within the AKR superfamily, the term AKR11B4 has been assigned to the enzyme. AKR11B4 is a biotechnologically attractive enzyme because of its broad substrate spectrum, combined with its distinctive regioselectivity and stereoselectivity. These features can be partially rationalized based on a 2-A crystal structure of apo-AKR11B4, which we describe and interpret here against the functional complex structures of other members of family 11 of the AKR superfamily. The structure of AKR11B4 shows the AKR-typical (beta/alpha)(8) TIM-barrel fold, with three loops and the C-terminal tail determining the particular enzymatic properties. In comparison to AKR11B1 (its closest AKR relative), AKR11B4 has a relatively broad binding cleft for the cosubstrate NADP/NADPH. In the crystalline environment, it is completely blocked by the C-terminal segment of a neighboring protomer. The structure reveals a conspicuous tryptophan residue (Trp23) that has to adopt an unconventional and strained side-chain conformation to permit cosubstrate binding. We predict and confirm by site-directed mutagenesis that Trp23 is an accelerator of (co)substrate turnover. Furthermore, we show that, simultaneously, this tryptophan residue is a critical determinant for substrate binding by the enzyme, while enantioselectivity is probably governed by a methionine residue within the C-terminal tail. We present structural reasons for these notions based on ternary complex models of AKR11B4, NADP, and either octanal, d-glyceraldehyde, or l-glyceraldehyde.

The Three-Dimensional Structure of AKR11B4, a Glycerol Dehydrogenase from Gluconobacter oxydans, Reveals a Tryptophan Residue as an Accelerator of Reaction Turnover.,Richter N, Breicha K, Hummel W, Niefind K J Mol Biol. 2010 Dec 3;404(3):353-62. Epub 2010 Sep 29. PMID:20887732<ref>PMID:20887732</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 3n2t" style="background-color:#fffaf0;"></div>

*[[Aldo-keto reductase|Aldo-keto reductase]]

[[Category: Breicha, K]]

[[Category: Hummel, W]]

[[Category: Niefind, K]]

[[Category: Richter, N]]

[[Category: Akr]]

[[Category: Akr11b4]]

[[Category: Tim barrel]]