1DOX
1H AND 15N SEQUENTIAL ASSIGNMENT, SECONDARY STRUCTURE AND TERTIARY FOLD OF [2FE-2S] FERREDOXIN FROM SYNECHOCYSTIS SP. PCC 6803
Summary for 1DOX
| Entry DOI | 10.2210/pdb1dox/pdb |
| Descriptor | FERREDOXIN [2FE-2S], FE2/S2 (INORGANIC) CLUSTER (2 entities in total) |
| Functional Keywords | iron-sulfur protein, electron transport |
| Biological source | Synechocystis sp. |
| Total number of polymer chains | 1 |
| Total formula weight | 10412.86 |
| Authors | Lelong, C.,Setif, P.,Bottin, H.,Andre, F.,Neumann, J.M. (deposition date: 1995-09-14, release date: 1996-03-08, Last modification date: 2024-04-10) |
| Primary citation | Lelong, C.,Setif, P.,Bottin, H.,Andre, F.,Neumann, J.M. 1H and 15N NMR sequential assignment, secondary structure, and tertiary fold of [2Fe-2S] ferredoxin from Synechocystis sp. PCC 6803. Biochemistry, 34:14462-14473, 1995 Cited by PubMed Abstract: The [2Fe-2S] ferredoxin extracted from Synechocystis sp. PCC 6803 was studied by 1H and 15N nuclear magnetic resonance. Sequence-specific 1H and 15N assignment of amino acid residues far from the paramagnetic cluster (distance higher than 8 A) was performed. Interresidue NOE constraints have allowed the identification of several secondary structure elements: one beta sheet composed of four beta strands, one alpha helix, and two alpha helix turns. The analysis of interresidue NOEs suggests the existence of a disulfide bridge between the cysteine residues 18 and 85. Such a disulfide bridge has never been observed in plant-type ferredoxins. Structure modeling using the X-PLOR program was performed with or without assuming the existence of a disulfide bridge. As a result, two structure families were obtained with rms deviations of 2.2 A. Due to the lack of NOE connectivities resulting from the paramagnetic effect from the [2Fe-2S] cluster, the structures were not well resolved in the region surrounding the [2Fe-2S] cluster, at both extremities of the alpha helix and the C and N terminus segments. In contrast, when taken separately, the beta sheet and the alpha helix were well defined. This work is the first report of a structure model of a plant-type [2Fe-2S] Fd in solution. PubMed: 7578051DOI: 10.1021/bi00044a024 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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