1zze
From Proteopedia
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[[Image:1zze.gif|left|200px]] | [[Image:1zze.gif|left|200px]] | ||
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| - | | | + | {{STRUCTURE_1zze| PDB=1zze | SCENE= }} |
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'''X-ray Structure of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor''' | '''X-ray Structure of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor''' | ||
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==Reference== | ==Reference== | ||
X-ray structures of NADPH-dependent carbonyl reductase from Sporobolomyces salmonicolor provide insights into stereoselective reductions of carbonyl compounds., Kamitori S, Iguchi A, Ohtaki A, Yamada M, Kita K, J Mol Biol. 2005 Sep 23;352(3):551-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16095619 16095619] | X-ray structures of NADPH-dependent carbonyl reductase from Sporobolomyces salmonicolor provide insights into stereoselective reductions of carbonyl compounds., Kamitori S, Iguchi A, Ohtaki A, Yamada M, Kita K, J Mol Biol. 2005 Sep 23;352(3):551-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16095619 16095619] | ||
| - | [[Category: Alcohol dehydrogenase (NADP(+))]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sporidiobolus salmonicolor]] | [[Category: Sporidiobolus salmonicolor]] | ||
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[[Category: Ohtaki, A.]] | [[Category: Ohtaki, A.]] | ||
[[Category: Yamada, M.]] | [[Category: Yamada, M.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:16:13 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:16, 3 May 2008
X-ray Structure of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor
Overview
The X-ray structures of red yeast Sporobolomyces salmonicolor carbonyl reductase (SSCR) and its complex with a coenzyme, NADPH, have been determined at a resolution of 1.8A and 1.6A, respectively. SSCR was crystallized in an orthorhombic system with the space group P2(1)2(1)2(1) and cell dimensions of a=54.86 A, b=83.49 A, and c=148.72 A. On its cocrystallization with NADPH, isomorphous crystals of the SSCR/NADPH complex were obtained. The structure of SSCR was solved by a single wavelength anomalous diffraction measurement using a selenomethionine-substituted enzyme, and that of the SSCR/NADPH complex was solved by a molecular replacement method using the solved structure of SSCR. The structures of SSCR and the SSCR/NADPH complex were refined to an R-factor of 0.193 (R(free)=0.233) and 0.211 (R(free)=0.238), respectively. SSCR has two domains, an NADPH-binding domain and a substrate-binding domain, and belongs to the short-chain dehydrogenases/reductases family. The structure of the NADPH-binding domain and the interaction between the enzyme and NADPH are very similar to those found in other structure-solved enzymes belonging to the short-chain dehydrogenases/reductases family, while the structure of the substrate-binding domain is unique. SSCR has stereoselectivity in its catalytic reaction, giving rise to excessive production of (S)-alcohols from ethyl 4-chloro-3-oxobutanoate. The X-ray structure of the SSCR/NADPH complex and preliminary modeling show that the formation of the hydrophobic channel induced by the binding of NADPH is closely related to the stereoselective reduction by SSCR.
About this Structure
1ZZE is a Single protein structure of sequence from Sporidiobolus salmonicolor. Full crystallographic information is available from OCA.
Reference
X-ray structures of NADPH-dependent carbonyl reductase from Sporobolomyces salmonicolor provide insights into stereoselective reductions of carbonyl compounds., Kamitori S, Iguchi A, Ohtaki A, Yamada M, Kita K, J Mol Biol. 2005 Sep 23;352(3):551-8. PMID:16095619 Page seeded by OCA on Sat May 3 18:16:13 2008
