Motion in Cytochrome P-450CAM [cc450cam]

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Classification Known Fragment Motion, Unclassifiable [F-?-2]

Structures
1FAG Conformation 1 [ PartsList ]
1PHA Conformation 2 [ PartsList ]
1PHB Conformation 3 [ PartsList ]
1PHC Conformation 4 [ PartsList ]
1PHD Conformation 5 [ PartsList ]
1PHE Conformation 6 [ PartsList ]
1PHF Conformation 7 [ PartsList ]
1PHG Conformation 8 [ PartsList ]

Description
In studies by Raag et al. (1993), the crystal structures of cytochrome P-450cam revealed dramatic structural changes of cytochrome P-450cam upon binding either of the enantiomeric inhibitor studied, suggesting that similiar changes occur upon binding of substrate. The motion involves primarily the Phe193, Tyr96, and Phe87 side chains. Tyr96 and Phe193 are observed to have 8.7 and 8.8 A displacements, respectively. The Phe96 side-chain also undergoes 80, 180, and -50 degree rotations around its side-chain C-beta, C-gamma, and the hydroxyphenyl ring, with respect to the camphor-bound enzyme. It is not clear from these studies how much backbone motion accompanies the side-chain rearrangements. At present it is not possible to classify this motion.

Particular values describing motion
Maximum atomic displacement (A) = 8.8 (For Phe193)
Experimental Methods = x (Traditional x-ray)
Creation Date = 19971130
Modification Date = 19971212

References
Raag R, Li H, Jones BC, Poulos TL (1993). Inhibitor-induced conformational change in cytochrome P-450CAM. Biochemistry 32(17):4571-4578. [Medline info for 93250020]
R Wade (1990). Solvation of the active site of cytochrome P450-cam. J. Comp. Aided Mol. Design. 4: 199-204. [Medline info for 93250020]

GO terms associated with structures
Molecular functionFMN binding, oxidoreductase activity, monooxygenase activity, electron transporter activity
Biological processelectron transport

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
cytochrome P450BM3 upload [ A ] upload [ A ] 455



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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu