4oxx

Crystal Structure of Cindoxin, Surface Entropy reduction Mutant

spinqualitylabelsall models 4oxx, resolution 1.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4oxx is a 1 chain structure with sequence from Citrobacter braakii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.21Å Ligands: FMN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CINC_CITBR Involved in the degradation of cineol (eucalyptol). The FMN protein, cindoxin, shuttles electrons between the FAD-containing cindoxin reductase (CinB) and 1,8-cineole 2-endo-monooxygenase (CinA). Publication Abstract from PubMed The crystal structure of the flavin mononucleotide (FMN)-containing redox partner to P450cin, cindoxin (Cdx), has been determined to 1.3 A resolution. The overall structure is similar to that of the FMN domain of human cytochrome P450 reductase. A Brownian dynamics-molecular dynamics docking method was used to produce a model of Cdx with its redox partner, P450cin. This Cdx-P450cin model highlights the potential importance of Cdx Tyr96 in bridging the FMN and heme cofactors as well P450cin Arg102 and Arg346. Each of the single-site Ala mutants exhibits approximately 10% of the wild-type activity, thus demonstrating the importance of these residues for binding and/or electron transfer. In the well-studied P450cam system, redox partner binding stabilizes the open low-spin conformation of P450cam and greatly decreases the stability of the oxy complex. In sharp contrast, Cdx does not shift P450cin to a low-spin state, although the stability of oxy-P450cin is decreased 10-fold in the presence of Cdx. This indicates that Cdx may have a modest effect on the open-closed equilibrium in P450cin compared to that in P450cam. It has been postulated that part of the effector role of Pdx on P450cam is to promote a significant structural change that makes available a proton relay network involving Asp251 required for O2 activation. The structure around the corresponding Asp in P450cin, Asp241, provides a possible structural reason for why P450cin is less dependent on its redox partner for functionally important structural changes. Crystal structure of cindoxin, the p450cin redox partner.,Madrona Y, Hollingsworth SA, Tripathi S, Fields JB, Rwigema JC, Tobias DJ, Poulos TL Biochemistry. 2014 Mar 11;53(9):1435-46. doi: 10.1021/bi500010m. Epub 2014 Feb, 25. PMID:24533927 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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