Conformational dynamics in cytochrome P450-substrate interactions.

H Li; T L Poulos

doi:10.1016/s0300-9084(97)82526-6

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PubMed · 9010597

Conformational dynamics in cytochrome P450-substrate interactions.

H Li·T L Poulos

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Abstract

There now are four known cytochrome P450 crystal structures. Two of these, P450cam and P450eryF, are substrate-bound while P450terp and the heme domain of P450BM-3 are substrate-free. Here we describe a preliminary analysis of the P450BM-3 heme domain complexed with the 16-carbon fatty acid substrate, palmitoleic acid. A comparison of the substrate-free and -bound structures shows that a large conformational change in the substrate access channel accompanies substrate binding. This new information, together with the substrate-bound structures of P450cam and P450eryF, reveals which regions of P450 are the most important in controlling the dynamics of substrate binding and recognition.

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Bacterial Proteins Binding Sites Crystallography, X-Ray Cytochrome P-450 Enzyme System Heme Mixed Function Oxygenases Molecular Structure NADPH-Ferrihemoprotein Reductase Protein Conformation Substrate Specificity Journal Article Research Support, U.S. Gov't, P.H.S.

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H Li, T L Poulos. 1996. Conformational dynamics in cytochrome P450-substrate interactions.. https://doi.org/10.1016/s0300-9084(97)82526-6

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