3WEC

Structure of P450 RauA (CYP1050A1) complexed with a biosynthetic intermediate of aurachin RE

Summary for 3WEC

• Entry DOI: 10.2210/pdb3wec/pdb
• Descriptor: Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, 3-[(2E,6E,9R)-9-hydroxy-3,7,11-trimethyldodeca-2,6,10-trien-1-yl]-2-methylquinolin-4(1H)-one, ... (4 entities in total)
• Functional Keywords: p450 fold, monooxygenase (hydroxylase), heme, cytosolic enzyme, oxidoreductase
• Biological source: Rhodococcus erythropolis
• Total number of polymer chains: 1
• Total formula weight: 46912.48

Authors

Yasutake, Y.,Kitagawa, W.,Tamura, T. (deposition date: 2013-07-03, release date: 2014-01-01, Last modification date: 2023-11-08)

Primary citation

Yasutake, Y.,Kitagawa, W.,Hata, M.,Nishioka, T.,Ozaki, T.,Nishiyama, M.,Kuzuyama, T.,Tamura, T.
Structure of the quinoline N-hydroxylating cytochrome P450 RauA, an essential enzyme that confers antibiotic activity on aurachin alkaloids
Febs Lett., 588:105-110, 2014

PubMed Abstract: The cytochrome P450 RauA from Rhodococcus erythropolis JCM 6824 catalyzes the hydroxylation of a nitrogen atom in the quinolone ring of aurachin, thereby conferring strong antibiotic activity on the aurachin alkaloid. Here, we report the crystal structure of RauA in complex with its substrate, a biosynthetic intermediate of aurachin RE. Clear electron density showed that the quinolone ring is oriented parallel to the porphyrin plane of the heme cofactor, while the farnesyl chain curls into a U-shape topology and is buried inside the solvent-inaccessible hydrophobic interior of RauA. The nearest atom from the heme iron is the quinolone nitrogen (4.3Å), which is consistent with RauA catalyzing the N-hydroxylation of the quinolone ring to produce mature aurachin RE.

PubMed: 24269679
DOI: 10.1016/j.febslet.2013.11.016

Experimental method

X-RAY DIFFRACTION (2.19 Å)