1y1p: Difference between revisions

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New page: left|200px<br /><applet load="1y1p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1y1p, resolution 1.60Å" /> '''X-ray structure of a...
 
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[[Image:1y1p.gif|left|200px]]<br /><applet load="1y1p" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1y1p, resolution 1.60&Aring;" />
'''X-ray structure of aldehyde reductase with NADPH'''<br />


==Overview==
==X-ray structure of aldehyde reductase with NADPH==
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.
<StructureSection load='1y1p' size='340' side='right'caption='[[1y1p]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1y1p]] 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=1Y1P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y1P FirstGlance]. <br>
1Y1P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sporidiobolus_salmonicolor Sporidiobolus salmonicolor] with SO4, ACT and NMN as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y1P OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=NMN:BETA-NICOTINAMIDE+RIBOSE+MONOPHOSPHATE'>NMN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1y1p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y1p OCA], [https://pdbe.org/1y1p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y1p RCSB], [https://www.ebi.ac.uk/pdbsum/1y1p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y1p ProSAT]</span></td></tr>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16095619 16095619]
</table>
[[Category: Alcohol dehydrogenase (NADP(+))]]
== Function ==
[[Category: Single protein]]
[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]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y1/1y1p_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1y1p ConSurf].
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sporidiobolus salmonicolor]]
[[Category: Sporidiobolus salmonicolor]]
[[Category: Kamitori, S.]]
[[Category: Kamitori S]]
[[Category: Kita, K.]]
[[Category: Kita K]]
[[Category: ACT]]
[[Category: NMN]]
[[Category: SO4]]
[[Category: rossmann fold]]
[[Category: short chain dehydrogenase reductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:29:46 2007''

Latest revision as of 13:37, 13 March 2024

X-ray structure of aldehyde reductase with NADPH

1y1p, resolution 1.60Å

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