2qbn: Difference between revisions

Revision as of 04:37, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2qbn.png

Template:STRUCTURE 2qbn

Crystal structure of ferric G248V cytochrome P450camCrystal structure of ferric G248V cytochrome P450cam

Template:ABSTRACT PUBMED 18001135

About this StructureAbout this Structure

2QBN is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

ReferenceReference

Alteration of P450 distal pocket solvent leads to impaired proton delivery and changes in heme geometry., Makris TM, von Koenig K, Schlichting I, Sligar SG, Biochemistry. 2007 Dec 11;46(49):14129-40. Epub 2007 Nov 15. PMID:18001135

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OCA

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-'''Crystal structure of ferric G248V cytochrome P450cam'''
+===Crystal structure of ferric G248V cytochrome P450cam===
-==Overview==
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-Distal pocket water molecules have been widely implicated in the delivery of protons required in O-O bond heterolysis in the P450 reaction cycle. Targeted dehydration of the cytochrome P450cam (CYP101) distal pocket through mutagenesis of a distal pocket glycine to either valine or threonine results in the alteration of spin state equilibria, and has dramatic consequences on the catalytic rate, coupling efficiency, and kinetic solvent isotope effect parameters, highlighting an important role of the active-site hydration level on P450 catalysis. Cryoradiolysis of the mutant CYP101 oxyferrous complexes further indicates a specific perturbation of proton-transfer events required for the transformation of ferric-peroxo to ferric-hydroperoxo states. Finally, crystallography of the 248Val and 248Thr mutants in both the ferric camphor bound resting state and ferric-cyano adducts shows both the alteration of hydrogen-bonding networks and the alteration of heme geometry parameters. Taken together, these results indicate that the distal pocket microenvironment governs the transformation of reactive heme-oxygen intermediates in P450 cytochromes.
+The line below this paragraph, {{ABSTRACT_PUBMED_18001135}}, adds the Publication Abstract to the page
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 [[Category: Heme geometry]]
 [[Category: Oxidoreductase]]
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