1zjy

<table><tr><td colspan='2'>[[1zjy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_casei_g"_von_freudenreich_and_thoni_1904 "bacillus casei g" von freudenreich and thoni 1904]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZJY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZJY FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene>, <scene name='pdbligand=SS2:(1R)-1-PHENYLETHANOL'>SS2</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nxq|1nxq]], [[1zjz|1zjz]], [[1zk0|1zk0]], [[1zk1|1zk1]], [[1zk2|1zk2]], [[1zk3|1zk3]], [[1zk4|1zk4]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </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=1zjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zjy OCA], [http://pdbe.org/1zjy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zjy RCSB], [http://www.ebi.ac.uk/pdbsum/1zjy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zjy ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The R-specific alcohol dehydrogenase (RADH) from Lactobacillus brevis is an NADP-dependent, homotetrameric member of the extended enzyme family of short-chain dehydrogenases/reductases (SDR) with a high biotechnological application potential. Its preferred in vitro substrates are prochiral ketones like acetophenone with almost invariably a small methyl group as one substituent and a bulky (often aromatic) moiety as the other. On the basis of an atomic-resolution structure of wild-type RADH in complex with NADP and acetophenone, we designed the mutant RADH-G37D, which should possess an improved cosubstrate specificity profile for biotechnological purposes, namely, a preference for NAD rather than NADP. Comparative kinetic measurements with wild-type and mutant RADH showed that this aim was achieved. To characterize the successful mutant structurally, we determined several, partly atomic-resolution, crystal structures of RADH-G37D both as an apo-enzyme and as ternary complex with NAD or NADH and phenylethanol. The increased affinity of RADH-G37D for NAD(H) depends on an interaction between the adenosine ribose moiety of NAD and the inserted aspartate side-chain. A structural comparison between RADH-G37D as apo-enzyme and as a part of a ternary complex revealed significant rearrangements of Ser141, Glu144, Tyr189 and Met205 in the vicinity of the active site. This plasticity contributes to generate a small hydrophobic pocket for the methyl group typical for RADH substrates, and a hydrophobic coat for the second, more variable and often aromatic, substituent. Around Ser141 we even found alternative conformations in the backbone. A structural adaptability in this region, which we describe here for the first time for an SDR enzyme, is probably functionally important, because it concerns Ser142, a member of the highly conserved catalytic tetrad typical for SDR enzymes. Moreover, it affects an extended proton relay system that has been identified recently as a critical element for the catalytic mechanism in SDR enzymes.

Atomic resolution structures of R-specific alcohol dehydrogenase from Lactobacillus brevis provide the structural bases of its substrate and cosubstrate specificity.,Schlieben NH, Niefind K, Muller J, Riebel B, Hummel W, Schomburg D J Mol Biol. 2005 Jun 17;349(4):801-13. PMID:15896805<ref>PMID:15896805</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 1zjy" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillus casei g von freudenreich and thoni 1904]]

[[Category: Hummel, W]]

[[Category: Muller, J]]

[[Category: Niefind, K]]

[[Category: Riebel, B]]

[[Category: Schlieben, N H]]

[[Category: Schomburg, D]]

[[Category: Short chain reductases/dehydrogenase]]