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1zze

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[[Image:1zze.gif|left|200px]]
 
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{{Structure
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==X-ray Structure of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor==
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|PDB= 1zze |SIZE=350|CAPTION= <scene name='initialview01'>1zze</scene>, resolution 1.80&Aring;
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<StructureSection load='1zze' size='340' side='right'caption='[[1zze]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1zze]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sporidiobolus_salmonicolor Sporidiobolus salmonicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZZE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZZE FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zze FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zze OCA], [https://pdbe.org/1zze PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zze RCSB], [https://www.ebi.ac.uk/pdbsum/1zze PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zze ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ALD2_SPOSA ALD2_SPOSA] Catalyzes the asymmetric reduction of o-substituted aliphatic and aromatic aldehydes and ketones to an S-enantiomer. Reduces ethyl 4-chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate.<ref>PMID:10583966</ref> [REFERENCE:2]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zz/1zze_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zze ConSurf].
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<div style="clear:both"></div>
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'''X-ray Structure of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor'''
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==See Also==
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*[[Carbonyl reductase 3D structures|Carbonyl reductase 3D structures]]
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== References ==
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==Overview==
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<references/>
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1ZZE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sporidiobolus_salmonicolor Sporidiobolus salmonicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZZE OCA].
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==Reference==
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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]
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[[Category: Alcohol dehydrogenase (NADP(+))]]
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[[Category: Single protein]]
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[[Category: Sporidiobolus salmonicolor]]
[[Category: Sporidiobolus salmonicolor]]
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[[Category: Iguchi, A.]]
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[[Category: Iguchi A]]
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[[Category: Kamitori, S.]]
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[[Category: Kamitori S]]
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[[Category: Kita, K.]]
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[[Category: Kita K]]
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[[Category: Ohtaki, A.]]
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[[Category: Ohtaki A]]
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[[Category: Yamada, M.]]
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[[Category: Yamada M]]
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[[Category: SO4]]
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[[Category: rosmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:41:42 2008''
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Current revision

X-ray Structure of NADPH-dependent Carbonyl Reductase from Sporobolomyces salmonicolor

PDB ID 1zze

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