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New page: left|200px<br /><applet load="1ae1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ae1, resolution 2.40Å" /> '''TROPINONE REDUCTASE-...
 
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[[Image:1ae1.gif|left|200px]]<br /><applet load="1ae1" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ae1, resolution 2.40&Aring;" />
'''TROPINONE REDUCTASE-I COMPLEX WITH NADP'''<br />


==Overview==
==TROPINONE REDUCTASE-I COMPLEX WITH NADP==
A pair of tropinone reductases (TRs) share 64% of the same amino acid, residues and belong to the short-chain dehydrogenase/reductase family. In, the synthesis of tropane alkaloids in several medicinal plants, the TRs, reduce a carbonyl group of an alkaloid intermediate, tropinone, to hydroxy, groups with different diastereomeric configurations. To clarify the, structural basis for their different reaction stereospecificities, we, determined the crystal structures of the two enzymes at 2.4- and 2.3-A, resolutions. The overall folding of the two enzymes was almost identical., The conservation was not confined within the core domains that are, conserved within the protein family but extended outside the core domain, where each family member has its characteristic structure. The binding, sites for the cofactor and the positions of the active site residues were, well conserved between the two TRs. The substrate binding site was, composed mostly of hydrophobic amino acids in both TRs, but the presence, of different charged residues conferred different electrostatic, environments on the two enzymes. A modeling study indicated that these, charged residues play a major role in controlling the binding orientation, of tropinone within the substrate binding site, thereby determining the, stereospecificity of the reaction product. The results obtained herein, raise the possibility that in certain cases different stereospecificities, can be acquired in enzymes by changing a few amino acid residues within, substrate binding sites.
<StructureSection load='1ae1' size='340' side='right'caption='[[1ae1]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1ae1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Datura_stramonium Datura stramonium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AE1 FirstGlance]. <br>
1AE1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Datura_stramonium Datura stramonium] with NAP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tropinone_reductase_II Tropinone reductase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.236 1.1.1.236] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AE1 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]] 2.4&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=1ae1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ae1 OCA], [https://pdbe.org/1ae1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ae1 RCSB], [https://www.ebi.ac.uk/pdbsum/1ae1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ae1 ProSAT]</span></td></tr>
Crystal structures of two tropinone reductases: different reaction stereospecificities in the same protein fold., Nakajima K, Yamashita A, Akama H, Nakatsu T, Kato H, Hashimoto T, Oda J, Yamada Y, Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4876-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9560196 9560196]
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRN1_DATST TRN1_DATST] Catalyzes the stereospecific reduction of tropinone to tropine.
== 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/ae/1ae1_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=1ae1 ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Datura stramonium]]
[[Category: Datura stramonium]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Tropinone reductase II]]
[[Category: Akama H]]
[[Category: Akama, H.]]
[[Category: Hashimoto T]]
[[Category: Hashimoto, T.]]
[[Category: Kato H]]
[[Category: Kato, H.]]
[[Category: Nakajima K]]
[[Category: Nakajima, K.]]
[[Category: Nakatsu T]]
[[Category: Nakatsu, T.]]
[[Category: Oda J]]
[[Category: Oda, J.]]
[[Category: Yamada Y]]
[[Category: Yamada, Y.]]
[[Category: Yamashita A]]
[[Category: Yamashita, A.]]
[[Category: NAP]]
[[Category: oxidoreductase]]
[[Category: reduction of tropinone to tropine]]
[[Category: short-chain dehydrogenase]]
[[Category: tropane alkaloid biosynthesis]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:47:11 2007''

Latest revision as of 06:29, 7 February 2024

TROPINONE REDUCTASE-I COMPLEX WITH NADP

1ae1, resolution 2.40Å

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