4jiq: Difference between revisions
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==Crystal structure of glycerol trinitrate reductase NerA from Agrobacterium radiobacter in complex with 1-nitro-2-phenylpropene== | ==Crystal structure of glycerol trinitrate reductase NerA from Agrobacterium radiobacter in complex with 1-nitro-2-phenylpropene== | ||
<StructureSection load='4jiq' size='340' side='right' caption='[[4jiq]], [[Resolution|resolution]] 2.49Å' scene=''> | <StructureSection load='4jiq' size='340' side='right'caption='[[4jiq]], [[Resolution|resolution]] 2.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jiq]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jiq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JIQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JIQ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1L5:[(1E)-1-NITROPROP-1-EN-2-YL]BENZENE'>1L5</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1L5:[(1E)-1-NITROPROP-1-EN-2-YL]BENZENE'>1L5</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4jiq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jiq OCA], [https://pdbe.org/4jiq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jiq RCSB], [https://www.ebi.ac.uk/pdbsum/4jiq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jiq ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/O31246_RHIRD O31246_RHIRD] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Agrobacterium tumefaciens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Gruber K]] | ||
[[Category: | [[Category: Oberdorfer G]] | ||
Revision as of 14:15, 24 November 2022
Crystal structure of glycerol trinitrate reductase NerA from Agrobacterium radiobacter in complex with 1-nitro-2-phenylpropeneCrystal structure of glycerol trinitrate reductase NerA from Agrobacterium radiobacter in complex with 1-nitro-2-phenylpropene
Structural highlights
FunctionPublication Abstract from PubMedIn recent years, Old Yellow Enzymes (OYEs) and their homologues have found broad application in the efficient asymmetric hydrogenation of activated CC bonds with high selectivities and yields. Members of this class of enzymes have been found in many different organisms and are rather diverse on the sequence level, with pairwise identities as low as 20 %, but they exhibit significant structural similarities with the adoption of a conserved (alphabeta)8 -barrel fold. Some OYEs have been shown not only to reduce CC double bonds, but also to be capable of reducing nitro groups in both saturated and unsaturated substrates. In order to understand this dual activity we determined and analyzed X-ray crystal structures of NerA from Agrobacterium radiobacter, both in its apo form and in complex with 4-hydroxybenzaldehyde and with 1-nitro-2-phenylpropene. These structures, together with spectroscopic studies of substrate binding to several OYEs, indicate that nitro-containing substrates can bind to OYEs in different binding modes, one of which leads to CC double bond reduction and the other to nitro group reduction. The Structure of Glycerol Trinitrate Reductase NerA from Agrobacterium radiobacter Reveals the Molecular Reason for Nitro- and Ene-Reductase Activity in OYE Homologues.,Oberdorfer G, Binter A, Wallner S, Durchschein K, Hall M, Faber K, Macheroux P, Gruber K Chembiochem. 2013 May 10;14(7):836-45. doi: 10.1002/cbic.201300136. Epub 2013 Apr, 18. PMID:23606302[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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