5ttk: Difference between revisions
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<StructureSection load='5ttk' size='340' side='right' caption='[[5ttk]], [[Resolution|resolution]] 2.51Å' scene=''> | <StructureSection load='5ttk' size='340' side='right' caption='[[5ttk]], [[Resolution|resolution]] 2.51Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ttk]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TTK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TTK FirstGlance]. <br> | <table><tr><td colspan='2'>[[5ttk]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Psep6 Psep6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TTK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TTK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ttj|5ttj]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ttj|5ttj]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPS_4081 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1042876 PSEP6])</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=5ttk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ttk OCA], [http://pdbe.org/5ttk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ttk RCSB], [http://www.ebi.ac.uk/pdbsum/5ttk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ttk ProSAT]</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=5ttk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ttk OCA], [http://pdbe.org/5ttk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ttk RCSB], [http://www.ebi.ac.uk/pdbsum/5ttk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ttk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Psep6]] | |||
[[Category: Allen, K N]] | [[Category: Allen, K N]] | ||
[[Category: Janda, K D]] | [[Category: Janda, K D]] | ||
Revision as of 17:27, 6 November 2017
Crystal Structure of Selenomethionine-incorporated Nicotine Oxidoreductase from Pseudomonas putidaCrystal Structure of Selenomethionine-incorporated Nicotine Oxidoreductase from Pseudomonas putida
Structural highlights
Publication Abstract from PubMedThe first structure of nicotine oxidoreductase (NicA2) was determined by X-ray crystallography. Pseudomonas putida has evolved nicotine-degrading activity to provide a source of carbon and nitrogen. The structure establishes NicA2 as a member of the monoamine oxidase family. Residues 1-50 are disordered and may play a role in localization. The nicotine-binding site proximal to the isoalloxazine ring of flavin shows an unusual composition of the classical aromatic cage (W427 and N462). The active site architecture is consistent with the proposed binding of the deprotonated form of the substrate and the flavin-dependent oxidation of the pyrrolidone C-N bond followed by nonenzymatic hydrolysis. Structural Analysis Provides Mechanistic Insight into Nicotine Oxidoreductase from Pseudomonas putida.,Tararina MA, Janda KD, Allen KN Biochemistry. 2016 Dec 6;55(48):6595-6598. Epub 2016 Nov 18. PMID:27933790[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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