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1nxq

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{{STRUCTURE_1nxq| PDB=1nxq | SCENE= }}
{{STRUCTURE_1nxq| PDB=1nxq | SCENE= }}
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'''Crystal Structure of R-alcohol dehydrogenase (RADH) (apoenyzme) from Lactobacillus brevis'''
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===Crystal Structure of R-alcohol dehydrogenase (RADH) (apoenyzme) from Lactobacillus brevis===
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==Overview==
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The crystal structure of the apo-form of an R-specific alcohol dehydrogenase from Lactobacillus brevis (LB-RADH) was solved and refined to 1.8A resolution. LB-RADH is a member of the short-chain dehydrogenase/reductase (SDR) enyzme superfamily. It is a homotetramer with 251 amino acid residues per subunit and uses NADP(H) as co-enzyme. NADPH and the substrate acetophenone were modelled into the active site. The enantiospecificity of the enzyme can be explained on the basis of the resulting hypothetical ternary complex. In contrast to most other SDR enzymes, the catalytic activity of LB-RADH depends strongly on the binding of Mg(2+). Mg(2+) removal by EDTA inactivates the enzyme completely. In the crystal structure, the Mg(2+)-binding site is well defined. The ion has a perfect octahedral coordination sphere and occupies a special position concerning crystallographic and molecular point symmetry, meaning that each RADH tetramer contains two magnesium ions. The magnesium ion is no direct catalytic cofactor. However, it is structurally coupled to the putative C-terminal hinge of the substrate-binding loop and, via an extended hydrogen bonding network, to some side-chains forming the substrate binding region. Therefore, the presented structure of apo-RADH provides plausible explanations for the metal dependence of the enzyme.
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(as it appears on PubMed at http://www.pubmed.gov), where 12628239 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12628239}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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]
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: Sdr enzyme family]]
[[Category: Sdr enzyme family]]
[[Category: Short chain dehydrogenases/reductase]]
[[Category: Short chain dehydrogenases/reductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:06:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:33:24 2008''

Revision as of 11:33, 27 July 2008

Image:1nxq.png

Template:STRUCTURE 1nxq

Crystal Structure of R-alcohol dehydrogenase (RADH) (apoenyzme) from Lactobacillus brevis

Template:ABSTRACT PUBMED 12628239

About this Structure

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

Reference

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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