THE SOLUTION NMR STRUCTURE OF OXIDIZED CYTOCHROME C6 FROM THE GREEN ALGA MONORAPHIDIUM BRAUNII, MINIMIZED AVERAGE STRUCTURE

File:1a2s.gif


1a2s

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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 ... [(full description)]

About this StructureAbout this Structure

1A2S is a [Single protein] structure of sequence from [Monoraphidium braunii] with HEC as [ligand]. Structure known Active Site: NUL. 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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