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PDBsum entry 1gdv

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Electron transport PDB id
1gdv
Contents
Protein chain
85 a.a. *
Ligands
HEC
Waters ×45
* Residue conservation analysis

References listed in PDB file
Key reference
Title Structure of cytochrome c6 from the red alga porphyra yezoensis at 1. 57 a resolution.
Authors S.Yamada, S.Y.Park, H.Shimizu, Y.Koshizuka, K.Kadokura, T.Satoh, K.Suruga, M.Ogawa, Y.Isogai, T.Nishio, Y.Shiro, T.Oku.
Ref. Acta Crystallogr D Biol Crystallogr, 2000, 56, 1577-1582. [DOI no: 10.1107/S090744490001461X]
PubMed id 11092924
Abstract
The crystal structure of cytochrome c(6) from the red alga Porphyra yezoensis has been determined at 1.57 A resolution. The crystal is tetragonal and belongs to space group P4(3)2(1)2, with unit-cell parameters a = b = 49.26 (3), c = 83.45 (4) A and one molecule per asymmetric unit. The structure was solved by the molecular-replacement method and refined with X-PLOR to an R factor of 19.9% and a free R factor of 25.4%. The overall structure of cytochrome c(6) follows the topology of class I c-type cytochromes in which the heme prosthetic group covalently binds to Cys14 and Cys17, and the iron has an octahedral coordination with His18 and Met58 as the axial ligands. The sequence and the structure of the eukaryotic red algal cytochrome c(6) are very similar to those of a prokaryotic cyanobacterial cytochrome c(6) rather than those of eukaryotic green algal c(6) cytochromes.
Figure 2.
Figure 2 The overall structure of P. yezoensis cytochrome c[6]. The helices and -sheets (colored pink) are indicated as thick ribbons and the helices I-IV are numbered. The N- and C-termini are indicated. The heme prosthetic group and the heme-binding residues (Cys14, Cys17, His18 and Met58) are represented by ball-and-stick models in the same coloring scheme as Fig. 1-. The figure is drawn with the solvent-exposed heme edge at the front (the His iron ligand being on the right).
Figure 3.
Figure 3 The structure around the exposed heme edge of the cytochrome c[6]. The ribbon model shows the protein region (residues 14-59). The heme is represented in pink and the heme iron by a grey ball. Met26, Lys29, Met41, Gln50 and Lys55 are represented by ball-and-stick models in the same coloring scheme as Fig. 1-. Water molecules are represented as red balls. Possible hydrogen bonds are indicated by red dashed lines.
The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2000, 56, 1577-1582) copyright 2000.
PROCHECK
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