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1zk1

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{{STRUCTURE_1zk1| PDB=1zk1 | SCENE= }}
{{STRUCTURE_1zk1| PDB=1zk1 | SCENE= }}
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'''Structure of R-specific alcohol dehydrogenase (mutant G37D) from Lactobacillus brevis in complex with phenylethanol and NAD'''
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===Structure of R-specific alcohol dehydrogenase (mutant G37D) from Lactobacillus brevis in complex with phenylethanol and NAD===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15896805}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15896805 15896805]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15896805 15896805]
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The crystal structure of R-specific alcohol dehydrogenase from Lactobacillus brevis suggests the structural basis of its metal dependency., Niefind K, Muller J, Riebel B, Hummel W, Schomburg D, J Mol Biol. 2003 Mar 21;327(2):317-28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12628239 12628239]
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Crystallization and preliminary characterization of crystals of R-alcohol dehydrogenase from Lactobacillus brevis., Niefind K, Riebel B, Muller J, Hummel W, Schomburg D, Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1696-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11092950 11092950]
[[Category: Lactobacillus brevis]]
[[Category: Lactobacillus brevis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: R-specific alcohol dehydrogenase]]
[[Category: R-specific alcohol dehydrogenase]]
[[Category: Short chain reductases/dehydrogenase]]
[[Category: Short chain reductases/dehydrogenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:43:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:33:23 2008''

Revision as of 13:33, 29 July 2008

Image:1zk1.png

Template:STRUCTURE 1zk1

Structure of R-specific alcohol dehydrogenase (mutant G37D) from Lactobacillus brevis in complex with phenylethanol and NAD

Template:ABSTRACT PUBMED 15896805

About this Structure

1ZK1 is a Single protein structure of sequence from Lactobacillus brevis. Full crystallographic information is available from OCA.

Reference

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

The crystal structure of R-specific alcohol dehydrogenase from Lactobacillus brevis suggests the structural basis of its metal dependency., Niefind K, Muller J, Riebel B, Hummel W, Schomburg D, J Mol Biol. 2003 Mar 21;327(2):317-28. PMID:12628239

Crystallization and preliminary characterization of crystals of R-alcohol dehydrogenase from Lactobacillus brevis., Niefind K, Riebel B, Muller J, Hummel W, Schomburg D, Acta Crystallogr D Biol Crystallogr. 2000 Dec;56(Pt 12):1696-8. PMID:11092950

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