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| - | [[Image:1zze.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1zze| PDB=1zze | SCENE= }} | | {{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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| - | ==Overview==
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| - | 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. |
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| | + | {{ABSTRACT_PUBMED_16095619}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[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
Template:STRUCTURE 1zze
X-ray Structure of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor
Template:ABSTRACT PUBMED 16095619
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 Tue Jul 29 03:15:53 2008
