PMID: 3768350Sep 9, 1986Paper

Crystal structure of substrate-free Pseudomonas putida cytochrome P-450

Biochemistry
T L PoulosA J Howard

Abstract

The crystal structure of Pseudomonas putida cytochrome P-450cam in the substrate-free form has been refined at 2.20-A resolution and compared to the substrate-bound form of the enzyme. In the absence of the substrate camphor, the P-450cam heme iron atom is hexacoordinate with the sulfur atom of Cys-357 providing one axial heme ligand and a water molecule or hydroxide ion providing the other axial ligand. A network of hydrogen-bonded solvent molecules occupies the substrate pocket in addition to the iron-linked aqua ligand. When a camphor molecule binds, the active site waters including the aqua ligand are displaced, resulting in a pentacoordinate high-spin heme iron atom. Analysis of the Fno camphor - F camphor difference Fourier and a quantitative comparison of the two refined structures reveal that no detectable conformational change results from camphor binding other than a small repositioning of a phenylalanine side chain that contacts the camphor molecule. However, large decreases in the mean temperature factors of three separate segments of the protein centered on Tyr-96, Thr-185, and Asp-251 result from camphor binding. This indicates that camphor binding decreases the flexibility in these three regions of the P-450cam m...Continue Reading

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Citations

Aug 6, 1998·Biopolymers·F NastriV Pavone
Jun 1, 1992·Journal of Computer-aided Molecular Design·D F Lewis, H Moereels
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Jun 5, 1987·Journal of Molecular Biology·T L PoulosA J Howard
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