'''X-ray Structure of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor'''
===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.
The line below this paragraph, {{ABSTRACT_PUBMED_16095619}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 16095619 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16095619}}
==About this Structure==
==About this Structure==
Line 28:
Line 32:
[[Category: Yamada, M.]]
[[Category: Yamada, M.]]
[[Category: Rosmann fold]]
[[Category: Rosmann fold]]
''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 Tue Jul 29 03:15:53 2008''
Revision as of 00:16, 29 July 2008
This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.
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
