1a2s
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THE SOLUTION NMR STRUCTURE OF OXIDIZED CYTOCHROME C6 FROM THE GREEN ALGA MONORAPHIDIUM BRAUNII, MINIMIZED AVERAGE STRUCTURE
OverviewOverview
Cytochrome c6 from Monoraphidium braunii, an 89-amino acid electron, transfer protein, has been investigated by NMR in solution, in its, oxidized form, at pH 7 and 300 K. By using a combination of COSY, TOCSY, and NOESY experiments, 84% of the proton resonances have been assigned. A, total of 1668 experimental NOE constraints, 1109 of which were meaningful, together with 288 pseudocontact shifts, have been used to determine the, structure in solution. This is represented as a family of 40 structures, which have been energy minimized. The rmsd values with respect to the mean, structure are 0.57 +/- 0.08 and 0.94 +/- 0.09 A for the backbone and heavy, atoms, respectively. The structure has been found to be very similar to, that of the reduced form, except for a rearrangement in propionate 7, a, feature which has been observed in all c-type cytochromes investigated so, far. Such a feature could be relevant for the efficiency of the electron, transfer pathway with either the oxidizing or the reducing partners. Other, differences in the oxidation states have been noted in the region proposed, to be involved in the interaction with the physiological partners.
About this StructureAbout this Structure
1A2S is a Single protein structure of sequence from Monoraphidium braunii with as ligand. Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of oxidized cytochrome c6 from the green alga Monoraphidium braunii., Banci L, Bertini I, De la Rosa MA, Koulougliotis D, Navarro JA, Walter O, Biochemistry. 1998 Apr 7;37(14):4831-43. PMID:9538000
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