1Y1P

X-ray structure of aldehyde reductase with NADPH

Summary for 1Y1P

• Entry DOI: 10.2210/pdb1y1p/pdb
• Related: 1UJM
• Descriptor: Aldehyde reductase II, SULFATE ION, ACETATE ION, ... (7 entities in total)
• Functional Keywords: rossmann fold, short chain dehydrogenase reductase, oxidoreductase
• Biological source: Sporidiobolus salmonicolor
• Total number of polymer chains: 2
• Total formula weight: 76256.40

Authors

Kamitori, S.,Kita, K. (deposition date: 2004-11-19, release date: 2005-09-06, Last modification date: 2024-03-13)

Primary citation

Kamitori, S.,Iguchi, A.,Ohtaki, A.,Yamada, M.,Kita, K.
X-ray Structures of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor Provide Insights into Stereoselective Reductions of Carbonyl Compounds
J.Mol.Biol., 352:551-558, 2005

PubMed Abstract: 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.

PubMed: 16095619
DOI: 10.1016/j.jmb.2005.07.011

Experimental method

X-RAY DIFFRACTION (1.6 Å)