3p80: Difference between revisions

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-[[Image:3p80.jpg|left|200px]]
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+==Pentaerythritol tetranitrate reductase co-crystal structure containing bound (E)-1-(3'-hydroxyphenyl)-2-nitroethene==
-The line below this paragraph, containing "STRUCTURE_3p80", creates the "Structure Box" on the page.
+<StructureSection load='3p80' size='340' side='right' caption='[[3p80]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3p80]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"aerobacter_cloacae"_(jordan_1890)_bergey_et_al._1923 "aerobacter cloacae" (jordan 1890) bergey et al. 1923]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P80 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P80 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=P80:3-[(E)-2-NITROETHENYL]PHENOL'>P80</scene></td></tr>
--->
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3p74|3p74]], [[3p7y|3p7y]], [[3p81|3p81]], [[3p82|3p82]], [[3p84|3p84]], [[3p8i|3p8i]], [[3p8j|3p8j]]</td></tr>
-{{STRUCTURE_3p80|  PDB=3p80  |  SCENE=  }}
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">onr, PETNR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=550 "Aerobacter cloacae" (Jordan 1890) Bergey et al. 1923])</td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NADPH_dehydrogenase NADPH dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.1 1.6.99.1] </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=3p80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p80 OCA], [http://pdbe.org/3p80 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3p80 RCSB], [http://www.ebi.ac.uk/pdbsum/3p80 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3p80 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+We have conducted a site-specific saturation mutagenesis study of H181 and H184 of flavoprotein pentaerythritol tetranitrate reductase (PETN reductase) to probe the role of these residues in substrate binding and catalysis with a variety of alpha,beta-unsaturated alkenes. Single mutations at these residues were sufficient to dramatically increase the enantiopurity of products formed by reduction of 2-phenyl-1-nitropropene. In addition, many mutants exhibited a switch in reactivity to predominantly catalyse nitro reduction, as opposed to CC reduction. These mutants showed an enhancement in a minor side reaction and formed 2-phenylpropanal oxime from 2-phenyl-1-nitropropene. The multiple binding conformations of hydroxy substituted nitro-olefins in PETN reductase were examined by using both structural and catalytic techniques. These compounds were found to bind in both active and inhibitory complexes; this highlights the plasticity of the active site and the ability of the H181/H184 couple to coordinate with multiple functional groups. These properties demonstrate the potential to use PETN reductase as a scaffold in the development of industrially useful biocatalysts.
-===Pentaerythritol tetranitrate reductase co-crystal structure containing bound (E)-1-(3'-hydroxyphenyl)-2-nitroethene===
+A Site-Saturated Mutagenesis Study of Pentaerythritol Tetranitrate Reductase Reveals that Residues 181 and 184 Influence Ligand Binding, Stereochemistry and Reactivity.,Toogood HS, Fryszkowska A, Hulley M, Sakuma M, Mansell D, Stephens GM, Gardiner JM, Scrutton NS Chembiochem. 2011 Mar 21;12(5):738-49. doi: 10.1002/cbic.201000662. Epub, 2011 Mar 4. PMID:21374779<ref>PMID:21374779</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3p80" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[3p80]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P80 OCA].
+*[[Pentaerythritol tetranitrate reductase|Pentaerythritol tetranitrate reductase]]
-[[Category: Enterobacter cloacae]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: NADPH dehydrogenase]]
-[[Category: Scrutton, N S.]]
+[[Category: Scrutton, N S]]
-[[Category: Toogood, H S.]]
+[[Category: Toogood, H S]]
+[[Category: Alpha]]
+[[Category: Beta barrel]]
+[[Category: Old Yellow Enzyme]]
+[[Category: Oxidoreductase]]