1PUT
AN NMR-DERIVED MODEL FOR THE SOLUTION STRUCTURE OF OXIDIZED PUTIDAREDOXIN, A 2FE, 2-S FERREDOXIN FROM PSEUDOMONAS
Summary for 1PUT
| Entry DOI | 10.2210/pdb1put/pdb |
| Descriptor | PUTIDAREDOXIN, FE2/S2 (INORGANIC) CLUSTER (2 entities in total) |
| Functional Keywords | electron transport |
| Biological source | Pseudomonas putida |
| Total number of polymer chains | 1 |
| Total formula weight | 11603.75 |
| Authors | Pochapsky, T.C.,Ye, X.M.,Ratnaswamy, G.,Lyons, T.A. (deposition date: 1994-07-09, release date: 1994-09-30, Last modification date: 2024-05-01) |
| Primary citation | Pochapsky, T.C.,Ye, X.M.,Ratnaswamy, G.,Lyons, T.A. An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas. Biochemistry, 33:6424-6432, 1994 Cited by PubMed Abstract: A model for the solution structure of oxidized putidaredoxin (Pdx), a 106-residue globular protein containing a Fe2S2 cluster, has been determined using homonuclear NMR methods. Pdx is the first of the class of Fe2S2Cys4 ferredoxins which act as electron-transfer partners for P-450 monooxygenases to be structurally characterized, and no crystal structure has been determined for Pdx or for any closely homologous protein. Pdx is the physiological redox partner of cytochrome P-450cam. A total of 878 NOE distance constraints, 66 phi angular constraints derived from NH-C alpha H coupling constants, and five paramagnetic broadening constraints were used in simulated annealing structural refinements to obtain a family of structures with pairwise rms deviations of 1.14 A for backbone atoms and 1.80 A for all non-hydrogen atoms. Paramagnetic broadening of resonances within a ca. 8-A radius of the metal cluster prevents the use of NMR-derived constraints in this region of the protein; structural constraints used to model the environment of the metal cluster were obtained from site-directed mutagenesis and model compounds and by comparison with known ferredoxin structures. Pdx retains a similar folding topology to other structurally characterized Fe2S2Cys4 ferredoxins but differs from the other ferredoxins in containing a significantly more compact structure in the C-terminal half of the protein. PubMed: 8204575DOI: 10.1021/bi00187a006 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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