5TJR

X-ray Crystal structure of a methylmalonate semialdehyde dehydrogenase from Pseudomonas sp. AAC

Summary for 5TJR

• Entry DOI: 10.2210/pdb5tjr/pdb
• Descriptor: Methylmalonate-semialdehyde dehydrogenase, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: dehydrogenase, industrial biotechnology, hexamer, oxidoreductase
• Biological source: Pseudomonas sp. AAC
• Total number of polymer chains: 6
• Total formula weight: 346200.94

Authors

Peat, T.S.,Newman, J. (deposition date: 2016-10-05, release date: 2017-01-11, Last modification date: 2023-10-04)

Primary citation

Tararina, M.A.,Janda, K.D.,Allen, K.N.
Structural Analysis Provides Mechanistic Insight into Nicotine Oxidoreductase from Pseudomonas putida.
Biochemistry, 55:6595-6598, 2016

PubMed Abstract: 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.

PubMed: 27933790
DOI: 10.1021/acs.biochem.6b00963

Experimental method

X-RAY DIFFRACTION (2.95 Å)