5mns | pdb_00005mns

Structural and functional characterization of OleP in complex with 6DEB in sodium formate

spinqualitylabelsall models 5mns, resolution 2.62Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mns is a 6 chain structure with sequence from Streptomyces antibioticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.62Å Ligands: DEB, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q59819_STRAT Publication Abstract from PubMed The regulation of cytochrome P450 activity is often achieved by structural transitions induced by substrate binding. We describe the conformational transition experienced upon binding by the P450 OleP, an epoxygenase involved in oleandomycin biosynthesis. OleP bound to the substrate analog 6DEB crystallized in 2 forms: one with an ensemble of open and closed conformations in the asymmetric unit and another with only the closed conformation. Characterization of OleP-6DEB binding kinetics, also using the P450 inhibitor clotrimazole, unveiled a complex binding mechanism that involves slow conformational rearrangement with the accumulation of a spectroscopically detectable intermediate where 6DEB is bound to open OleP. Data reported herein provide structural snapshots of key precatalytic steps in the OleP reaction and explain how structural rearrangements induced by substrate binding regulate activity.-Parisi, G., Montemiglio, L. C., Giuffre, A., Macone, A., Scaglione, A., Cerutti, G., Exertier, C., Savino, C., Vallone, B. Substrate-induced conformational change in cytochrome P450 OleP. Substrate-induced conformational change in cytochrome P450 OleP.,Parisi G, Montemiglio LC, Giuffre A, Macone A, Scaglione A, Cerutti G, Exertier C, Savino C, Vallone B FASEB J. 2018 Sep 12:fj201800450RR. doi: 10.1096/fj.201800450RR. PMID:30207799 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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