PDBsum entry 1kib

Electron transport

PDB id: 1kib

Contents

Protein chains

(+ 2 more) 89 a.a. *

Ligands

HEC ×8

* Residue conservation analysis

PDB id:

1kib

Name:

Electron transport

Title:

Cytochrome c6 from arthrospira maxima: an assembly of 24 subunits in the form of an oblate shell

Structure:

Cytochrome c6. Chain: a, b, c, d, e, f, g, h. Synonym: soluble cytochrome f, cytochrome c553

Source:

Arthrospira maxima. Organism_taxid: 129910

Biol. unit:

24mer (from PDB file)

Resolution:

3.50Å R-factor: 0.204 R-free: 0.223

Authors:

C.A.Kerfeld,M.R.Sawaya,D.Krogmann,T.O.Yeates

Key ref:

C.A.Kerfeld et al. (2002). Structure of cytochrome c6 from Arthrospira maxima: an assembly of 24 subunits in a nearly symmetric shell. Acta Crystallogr D Biol Crystallogr, 58, 1104-1110. PubMed id: 12077429 DOI: 10.1107/S0907444902006534

Date:

03-Dec-01 Release date: 03-Jul-02

Protein chains

P00118  (CYC6_LIMMA) -  Cytochrome c6 from Limnospira maxima

Seq: 89 a.a.

Struc: 89 a.a.

DOI no: 10.1107/S0907444902006534

Acta Crystallogr D Biol Crystallogr 58:1104-1110 (2002)

PubMed id: 12077429

Structure of cytochrome c6 from Arthrospira maxima: an assembly of 24 subunits in a nearly symmetric shell.

C.A.Kerfeld, M.R.Sawaya, D.W.Krogmann, T.O.Yeates.

ABSTRACT

Cytochrome c(6) from the cyanobacterium Arthrospira maxima is present in isoforms that can be resolved by size-exclusion chromatography. One isoform crystallized in space group I4(1)32 with eight protein molecules in the asymmetric unit and a total of 384 molecules in the unit cell. Within the crystal, the molecules are arranged as clusters of 24 cytochrome c(6) molecules. Each cluster is a hollow shell with approximate octahedral (432) symmetry. Structural and biochemical studies of cytochrome c(6) isolated from other cyanobacteria and algae have led to the suggestion that cytochrome c(6) forms oligomers. The cytochrome c(6) complex described here is the largest assembly of cytochrome c(6) molecules observed thus far.

Selected figure(s)

Figure 2.
Figure 2 The A. maxima cytochrome c[6] 24-molecule cluster, viewed down the (a) threefold and (b) pseudo-fourfold axis. In (b) the side chains of Met19 which flank the pore are shown. This figure and Figs. 3-and 5-(a) were drawn with RIBBONS (Carson, 1997[Carson, M. (1997). Methods Enzymol. 277, 493-505.]).

Figure 5.
Figure 5 (a) Comparison of the A. maxima cytochrome c[6] trimer to trimers observed in the crystal structures of C. reinhardtii (Kerfeld et al., 1995[Kerfeld, C. A., Anwar, H. P., Interrante, R., Merchant, S. & Yeates, T. O. (1995). J. Mol. Biol. 250, 627-647.]) and M. braunii (Frazao et al., 1995[Frazao, C., Soares, C. M., Carrondo, M. A., Pohl, E., Dauter, Z., Wilson, K. S., Hervas, M., Navarro, J. A., De la Rosa, M. A. & Sheldrick, G. M. (1995). Structure, 3, 1159-1169.]) cytochrome c[6]. (b) and (c) Comparison of the electrostatic surface potential of the trimers. The view shown in (b) is the same as in (a); the view shown in (c) shows the opposite face.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2002, 58, 1104-1110) copyright 2002.

Figures were selected by the author.