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High-resolution crystal structure of the electron transfer complex of cytochrome p450cam with putidaredoxin
Structural highlights
FunctionCPXA_PSEPU Involved in a camphor oxidation system. Publication Abstract from PubMedWell-defined, stereospecific states in protein complexes are often in exchange with an ensemble of more dynamic orientations: the encounter states. The structure of the stereospecific complex between cytochrome P450cam and putidaredoxin was solved recently by X-ray diffraction as well as paramagnetic NMR spectroscopy. Other than the stereospecific complex, the NMR data clearly show the presence of additional states in the complex in solution. In these encounter states, populated for a small percentage of the time, putidaredoxin assumes multiple orientations and samples a large part of the surface of cytochrome P450cam. To characterize the nature of the encounter states, an extensive paramagnetic NMR dataset has been analyzed using the Maximum Occurrence of Regions methodology. The analysis reveals the location and maximal spatial extent of the additional states needed to fully explain the NMR data. Under the assumption of sparsity of the size of the conformational ensemble, several minor states can be located quite precisely. The distribution of these minor states correlates with the electrostatic potential map around cytochrome P450cam. Whereas some minor states are on isolated positively charged patches, others are connected to the stereospecific site via positively charged paths. The existence of electrostatically favorable pathways between the stereospecific interaction site and the different minor states or lack thereof suggests a means to discriminate between productive and futile encounter states. Identification of productive and futile encounters in an electron transfer protein complex.,Andralojc W, Hiruma Y, Liu WM, Ravera E, Nojiri M, Parigi G, Luchinat C, Ubbink M Proc Natl Acad Sci U S A. 2017 Mar 7;114(10):E1840-E1847. doi:, 10.1073/pnas.1616813114. Epub 2017 Feb 21. PMID:28223532[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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