2rfc | pdb_00002rfc

Ligand bound (4-phenylimidazole) Crystal Structure of a Cytochrome P450 from the Thermoacidophilic Archaeon Picrophilus Torridus

spinqualitylabelsall models 2rfc, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2rfc is a 4 chain structure with sequence from Picrophilus oshimae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: HEM, PIM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6KZ68_PICTO Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of a cytochrome P450 from the thermoacidophile Picrophilus torridus, CYP231A2 (PTO1399), has been solved. This structure reveals a wide open substrate access channel. To better understand ligand-induced structural transitions in CYP231A2, protein-ligand interactions were investigated using 4-phenylimidazole. Comparison of the ligand-free and -bound CYP231A2 structures shows conformational changes where the F and G helices swing as a single rigid body about a pivot point at the N-terminal end of the F helix, allowing the F helix region to dip toward the heme, resulting in closer contacts with the ligand. Thermal melting data illustrate that the melting temperature for CYP231A2 increases nearly 10 degrees C upon ligand binding, thus illustrating that the closed conformation is substantially more stable. Furthermore, spectroscopic data indicate that the active site is stable at pH 4.5, although, unusually, the thiolate ligand to the iron can be reversibly protonated. CYP231A2 does not exhibit structural features normally associated with thermophilic proteins such as an increase in salt bridge networks or extensive aromatic clustering. The increase in thermal stability instead is best correlated with the smaller size and shorter loops in CYP231A2 compared to other P450s. Crystal Structure and Properties of CYP231A2 from the Thermoacidophilic Archaeon Picrophilus torridus(,).,Ho WW, Li H, Nishida CR, Montellano PR, Poulos TL Biochemistry. 2008 Feb 19;47(7):2071-9. Epub 2008 Jan 16. PMID:18197710 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cytochrome P450 3D structures

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