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==X-ray Crystal structure of a methylmalonate semialdehyde dehydrogenase from Pseudomonas sp. AAC== | |||
<StructureSection load='5tjr' size='340' side='right'caption='[[5tjr]], [[Resolution|resolution]] 2.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5tjr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._AAC Pseudomonas sp. AAC]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TJR FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</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=5tjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tjr OCA], [https://pdbe.org/5tjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tjr RCSB], [https://www.ebi.ac.uk/pdbsum/5tjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tjr ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:27933790</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5tjr" style="background-color:#fffaf0;"></div> | ||
[[Category: Newman | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas sp. AAC]] | |||
[[Category: Newman J]] | |||
[[Category: Peat TS]] | |||
Latest revision as of 16:03, 4 October 2023
X-ray Crystal structure of a methylmalonate semialdehyde dehydrogenase from Pseudomonas sp. AACX-ray Crystal structure of a methylmalonate semialdehyde dehydrogenase from Pseudomonas sp. AAC
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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