6NBL
Cytochrome P450cam-putidaredoxin complex bound to camphor and cyanide
Summary for 6NBL
| Entry DOI | 10.2210/pdb6nbl/pdb |
| Descriptor | Camphor 5-monooxygenase, Putidaredoxin, PROTOPORPHYRIN IX CONTAINING FE, ... (9 entities in total) |
| Functional Keywords | electron transport, oxidoreductase |
| Biological source | Pseudomonas putida More |
| Total number of polymer chains | 4 |
| Total formula weight | 120236.90 |
| Authors | Follmer, A.H.,Tripathi, S.M.,Poulos, T.L. (deposition date: 2018-12-07, release date: 2019-03-06, Last modification date: 2024-12-25) |
| Primary citation | Follmer, A.H.,Tripathi, S.,Poulos, T.L. Ligand and Redox Partner Binding Generates a New Conformational State in Cytochrome P450cam (CYP101A1). J. Am. Chem. Soc., 141:2678-2683, 2019 Cited by PubMed Abstract: 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)═O 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 O 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. PubMed: 30672701DOI: 10.1021/jacs.8b13079 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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