1phc
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| , resolution 1.6Å | |||||||
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| Ligands: | |||||||
| Activity: | Camphor 5-monooxygenase, with EC number 1.14.15.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF SUBSTRATE-FREE PSEUDOMONAS PUTIDA CYTOCHROME P450
OverviewOverview
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 molecule without altering the mean position of the atoms involved.
About this StructureAbout this Structure
1PHC is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of substrate-free Pseudomonas putida cytochrome P-450., Poulos TL, Finzel BC, Howard AJ, Biochemistry. 1986 Sep 9;25(18):5314-22. PMID:3768350
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