9BW8

Structure of P450Blt from Micromonospora sp. MW-13 in Complex with Fluorinated Biarylitide

Summary for 9BW8

Entry DOI	10.2210/pdb9bw8/pdb
Descriptor	Cytochrome P450-SU1, Fluorinated Biarylitide, trifluoroacetic acid, ... (6 entities in total)
Functional Keywords	complex, biarylitide, crosslink, oxidoreductase
Biological source	Micromonospora sp. MW-13 More
Total number of polymer chains	4
Total formula weight	139178.26
Authors	Hansen, M.H.,Cryle, M.J.,Zhao, Y. (deposition date: 2024-05-21, release date: 2024-11-20, Last modification date: 2024-11-27)
Primary citation	Zhao, Y.,Gullick, J.,Hansen, M.H.,Coe, L.,Treisman, M.,Schittenhelm, R.B.,McKay, A.,Murray, L.A.M.,Tailhades, J.,De Voss, J.J.,Krenske, E.H.,Cryle, M.J. Loss of fluorine during crosslinking by the biarylitide P450 Blt proceeds due to restricted peptide orientation. Chem.Commun.(Camb.), 60:13951-13954, 2024 Cited by PubMed Abstract: The biarylitide crosslinking enzyme P450 can perform crosslinking between -F-Tyr-3 and His-5 residues within peptide substrates with concomitant and specific loss of fluorine. Our investigations suggest that a small intrinsic preference for coupling to fluorine is magnified by the binding of the peptide in a specific orientation that enforces the loss of fluorine during peptide crosslinking, likely a two-step reaction mechanism involving the non-enzyme catalysed reductive elimination of fluoride. PubMed: 39512132 DOI: 10.1039/d4cc04092a PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.86 Å)

Structure validation