2OLN

NikD, an unusual amino acid oxidase essential for nikkomycin biosynthesis: closed form at 1.15 A resolution

Summary for 2OLN

• Entry DOI: 10.2210/pdb2oln/pdb
• Related: 2OLN 2OLO
• Descriptor: nikD protein, SODIUM ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: flavoprotein, rossmann fold, oxidoreductase
• Biological source: Streptomyces tendae
• Total number of polymer chains: 1
• Total formula weight: 45102.14

Authors

Carrell, C.J.,Bruckner, R.C.,Venci, D.,Zhao, G.,Jorns, M.S.,Mathews, F.S. (deposition date: 2007-01-19, release date: 2007-07-31, Last modification date: 2024-10-30)

Primary citation

Carrell, C.J.,Bruckner, R.C.,Venci, D.,Zhao, G.,Jorns, M.S.,Mathews, F.S.
NikD, an unusual amino acid oxidase essential for nikkomycin biosynthesis: structures of closed and open forms at 1.15 and 1.90 A resolution
Structure, 15:928-941, 2007

PubMed Abstract: NikD is an unusual amino-acid-oxidizing enzyme that contains covalently bound FAD, catalyzes a 4-electron oxidation of piperideine-2-carboxylic acid to picolinate, and plays a critical role in the biosynthesis of nikkomycin antibiotics. Crystal structures of closed and open forms of nikD, a two-domain enzyme, have been determined to resolutions of 1.15 and 1.9 A, respectively. The two forms differ by an 11 degrees rotation of the catalytic domain with respect to the FAD-binding domain. The active site is inaccessible to solvent in the closed form; an endogenous ligand, believed to be picolinate, is bound close to and parallel with the flavin ring, an orientation compatible with redox catalysis. The active site is solvent accessible in the open form, but the picolinate ligand is approximately perpendicular to the flavin ring and a tryptophan is stacked above the flavin ring. NikD also contains a mobile cation binding loop.

PubMed: 17697998
DOI: 10.1016/j.str.2007.06.010

Experimental method

X-RAY DIFFRACTION (1.15 Å)