3SM8

Crystal Structure of Pseudomonas aeruginosa D-Arginine Dehydrogenase in Complex with an (N5) Flavin Adduct

Summary for 3SM8

• Entry DOI: 10.2210/pdb3sm8/pdb
• Related: 3NYC 3NYE 3NYF
• Descriptor: FAD-dependent catabolic D-arginine dehydrogenase, DauA, GLYCEROL, [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-5-[7,8-dimethyl-5-(3-methylbutanoyl)-2,4-dioxo-1,3,4,5-tetrahydrobenzo[g]pteridin-10(2H)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate, ... (4 entities in total)
• Functional Keywords: n(5) flavin adduct, oxidoreductase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 42553.47

Authors

Fu, G.,Weber, I.T. (deposition date: 2011-06-27, release date: 2011-07-20, Last modification date: 2024-04-03)

Primary citation

Fu, G.,Yuan, H.,Wang, S.,Gadda, G.,Weber, I.T.
Atomic-resolution structure of an N5 flavin adduct in D-arginine dehydrogenase.
Biochemistry, 50:6292-6294, 2011

PubMed Abstract: D-Arginine dehydrogenase (DADH) catalyzes the flavin-dependent oxidative deamination of D-arginine and other D-amino acids to the corresponding imino acids. The 1.07 Å atomic-resolution structure of DADH crystallized with D-leucine unexpectedly revealed a covalent N(5) flavin adduct, instead of the expected iminoleucine product in the active site. This acyl adduct has been successfully reproduced by photoreduction of DADH in the presence of 4-methyl-2-oxopentanoic acid (ketoleucine). The iminoleucine may be released readily because of weak interactions in the binding site, in contrast to iminoarginine, converted to ketoleucine, which reacts with activated FAD to form the covalently linked acyl adduct.

PubMed: 21707047
DOI: 10.1021/bi200831a

Experimental method

X-RAY DIFFRACTION (1.07 Å)