1VM9
The X-ray Structure of the cys84ala cys85ala double mutant of the [2Fe-2S] Ferredoxin subunit of Toluene-4-Monooxygenase from Pseudomonas Mendocina KR1
Summary for 1VM9
| Entry DOI | 10.2210/pdb1vm9/pdb |
| Descriptor | Toluene-4-monooxygenase system protein C, MAGNESIUM ION, FE2/S2 (INORGANIC) CLUSTER, ... (5 entities in total) |
| Functional Keywords | structural genomics, cesg, protein structure initiative, psi, ferredoxin, fes, [2fe-2s] cluster, rieske protein, toluene-4-monooxygenase subunit, center for eukaryotic structural genomics, electron transport |
| Biological source | Pseudomonas mendocina |
| Total number of polymer chains | 1 |
| Total formula weight | 12552.00 |
| Authors | Wesenberg, G.E.,Smith, D.W.,Phillips Jr., G.N.,Bingman, C.A.,Allard, S.T.M.,Moe, L.A.,Fox, B.G.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2004-09-13, release date: 2004-09-21, Last modification date: 2023-12-27) |
| Primary citation | Moe, L.A.,Bingman, C.A.,Wesenberg, G.E.,Phillips, G.N.,Fox, B.G. Structure of T4moC, the Rieske-type ferredoxin component of toluene 4-monooxygenase. Acta Crystallogr.,Sect.D, 62:476-482, 2006 Cited by PubMed Abstract: The structure of the Rieske-type ferredoxin (T4moC) from toluene 4-monooxygenase was determined by X-ray crystallography in the [2Fe-2S](2+) state at a resolution of 1.48 A using single-wavelength anomalous dispersion phasing with the [2Fe-2S] center. The structure consists of ten beta-strands arranged into the three antiparallel beta-sheet topology observed in all Rieske proteins. Trp69 of T4moC is adjacent to the [2Fe-2S] centre, which displaces a loop containing the conserved Pro81 by approximately 8 A away from the [2Fe-2S] cluster compared with the Pro loop in the closest structural and functional homolog, the Rieske-type ferredoxin BphF from biphenyl dioxygenase. In addition, T4moC contains five hydrogen bonds to the [2Fe-2S] cluster compared with three hydrogen bonds in BphF. Moreover, the electrostatic surface of T4moC is distinct from that of BphF. These structural differences are identified as possible contributors to the evolutionary specialization of soluble Rieske-type ferredoxins between the diiron monooxygenases and cis-dihydrodiol-forming dioxygenases. PubMed: 16627939DOI: 10.1107/S0907444906006056 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.48 Å) |
Structure validation
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