4d3d

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d3d RCSB], [http://www.ebi.ac.uk/pdbsum/4d3d PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d3d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4d3d RCSB], [http://www.ebi.ac.uk/pdbsum/4d3d PDBsum]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Oxidoreductases from Streptomyces sp. GF3546 [3546-IRED], Bacillus cereus BAG3X2 (BcIRED) and Nocardiopsis halophila (NhIRED) each reduce prochiral 2-methylpyrroline (2MPN) to (S)-2-methylpyrrolidine with &gt;95 % ee and also a number of other imine substrates with good selectivity. Structures of BcIRED and NhIRED have helped to identify conserved active site residues within this subgroup of imine reductases that have S selectivity towards 2MPN, including a tyrosine residue that has a possible role in catalysis and superimposes with an aspartate in related enzymes that display R selectivity towards the same substrate. Mutation of this tyrosine residue-Tyr169-in 3546-IRED to Phe resulted in a mutant of negligible activity. The data together provide structural evidence for the location and significance of the Tyr residue in this group of imine reductases, and permit a comparison of the active sites of enzymes that reduce 2MPN with either R or S selectivity.
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Structure, Activity and Stereoselectivity of NADPH-Dependent Oxidoreductases Catalysing the S-Selective Reduction of the Imine Substrate 2-Methylpyrroline.,Man H, Wells E, Hussain S, Leipold F, Hart S, Turkenburg JP, Turner NJ, Grogan G Chembiochem. 2015 Mar 24. doi: 10.1002/cbic.201402625. PMID:25809902<ref>PMID:25809902</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 05:38, 8 April 2015

Structure of Imine Reductase BcSIRED from Bacillus cereus BAG3X2

4d3d, resolution 1.71Å

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