3SM8: Crystal Structure Of Pseudomonas Aeruginosa D-Arginine Dehydrogenase In Complex With An (N5) Flavin Adduct

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 A 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.
PDB ID: 3SM8Download
MMDB ID: 92227
PDB Deposition Date: 2011/6/27
Updated in MMDB: 2011/07
Experimental Method:
x-ray diffraction
Resolution: 1.07  Å
Source Organism:
Similar Structures:
Biological Unit for 3SM8: monomeric; determined by author and by software (PISA)
Molecular Components in 3SM8
Label Count Molecule
Protein (1 molecule)
Fad-dependent Catabolic D-arginine Dehydrogenase, Daua(Gene symbol: dauA)
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB