PDBsum entry 1a2s

Electron transport

PDB id: 1a2s

Contents

Protein chain

89 a.a. *

Ligands

HEC

* Residue conservation analysis

PDB id:

1a2s

Name:

Electron transport

Title:

The solution nmr structure of oxidized cytochrome c6 from the green alga monoraphidium braunii, minimized average structure

Structure:

Cytochrome c6. Chain: a. Synonym: cytochrome c552. Other_details: oxidized form

Source:

Monoraphidium braunii. Organism_taxid: 34112

NMR struc:

1 models

Authors:

L.Banci,I.Bertini,M.A.De La Rosa,D.Koulougliotis,J.A.Navarro,O.Walter

Key ref:

L.Banci et al. (1998). Solution structure of oxidized cytochrome c6 from the green alga Monoraphidium braunii. Biochemistry, 37, 4831-4843. PubMed id: 9538000 DOI: 10.1021/bi972765y

Date:

10-Jan-98 Release date: 29-Apr-98

Protein chain

Q09099  (CYC6_MONBR) -  Cytochrome c6 from Chlorolobion braunii

Seq: 89 a.a.

Struc: 89 a.a.

DOI no: 10.1021/bi972765y

Biochemistry 37:4831-4843 (1998)

PubMed id: 9538000

Solution structure of oxidized cytochrome c6 from the green alga Monoraphidium braunii.

L.Banci, I.Bertini, M.A.De la Rosa, D.Koulougliotis, J.A.Navarro, O.Walter.

ABSTRACT

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.