4OXX
Crystal Structure of Cindoxin, Surface Entropy reduction Mutant
Summary for 4OXX
| Entry DOI | 10.2210/pdb4oxx/pdb |
| Descriptor | Cindoxin, FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | flavoprotein, fmn, cindoxin, electron transport |
| Biological source | Citrobacter braakii |
| Total number of polymer chains | 1 |
| Total formula weight | 17327.83 |
| Authors | Madrona, Y.,Poulos, T.L. (deposition date: 2014-02-07, release date: 2014-04-16, Last modification date: 2023-12-27) |
| Primary citation | Madrona, Y.,Hollingsworth, S.A.,Tripathi, S.,Fields, J.B.,Rwigema, J.C.,Tobias, D.J.,Poulos, T.L. Crystal structure of cindoxin, the P450cin redox partner. Biochemistry, 53:1435-1446, 2014 Cited by PubMed Abstract: The crystal structure of the flavin mononucleotide (FMN)-containing redox partner to P450cin, cindoxin (Cdx), has been determined to 1.3 Å 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 ~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. PubMed: 24533927DOI: 10.1021/bi500010m PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.21 Å) |
Structure validation
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