6nbl

Cytochrome P450cam-putidaredoxin complex bound to camphor and cyanide

spinqualitylabelsall models 6nbl, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6nbl is a 4 chain structure with sequence from Pseudomonas putida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.15Å Ligands: 1N0, CA, CAM, CYN, FES, HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CPXA_PSEPU Involved in a camphor oxidation system. Publication Abstract from PubMed It has become increasingly clear that cytochromes P450 can cycle back and forth between two extreme conformational states termed the closed and open states. In the well-studied cytochrome P450cam, the binding of its redox partner, putidaredoxin (Pdx), shifts P450cam toward the open state. Shifting to the open state is thought to be important in the formation of a proton relay network essential for O-O bond cleavage and formation of the active Fe(IV) horizontal lineO intermediate. Another important intermediate is the oxy-P450cam complex when bound to Pdx. Trapping this intermediate in crystallo is challenging owing to its instability, but the CN(-) complex is both stable and an excellent mimic of the O2 complex. Here we present the P450cam-Pdx structure complexed with CN(-). CN(-) results in large conformational changes including cis/trans isomerization of proline residues. Changes include large rearrangements of active-site residues and the formation of new active-site access channel that we have termed channel 2. The formation of channel 2 has also been observed in our previous molecular dynamics simulations wherein substrate binding to an allosteric site remote from the active site opens up channel 2. This new structure supports an extensive amount of previous work showing that distant regions of the structure are dynamically coupled and underscores the potentially important role that large conformational changes and dynamics play in P450 catalysis. Ligand and Redox Partner Binding Generates a New Conformational State in Cytochrome P450cam (CYP101A1).,Follmer AH, Tripathi S, Poulos TL J Am Chem Soc. 2019 Feb 13;141(6):2678-2683. doi: 10.1021/jacs.8b13079. Epub 2019, Jan 31. PMID:30672701 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ferredoxin 3D structures

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