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PDBsum entry 1f1f

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Electron transport PDB id
1f1f

 

 

 

 

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Contents
Protein chain
88 a.a. *
Ligands
HEC
* Residue conservation analysis
PDB id:
1f1f
Name: Electron transport
Title: Crystal structure of cytochrome c6 from arthrospira maxima
Structure: Cytochrome c6. Chain: a
Source: Arthrospira maxima. Organism_taxid: 129910
Resolution:
2.70Å     R-factor:   0.232     R-free:   0.255
Authors: C.A.Kerfeld,A.A.Serag,M.R.Sawaya,D.W.Krogmann,T.O.Yeates
Key ref:
M.R.Sawaya et al. (2001). Structures of cytochrome c-549 and cytochrome c6 from the cyanobacterium Arthrospira maxima. Biochemistry, 40, 9215-9225. PubMed id: 11478889 DOI: 10.1021/bi002679p
Date:
18-May-00     Release date:   08-Aug-01    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00118  (CYC6_LIMMA) -  Cytochrome c6 from Limnospira maxima
Seq:
Struc:
89 a.a.
88 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1021/bi002679p Biochemistry 40:9215-9225 (2001)
PubMed id: 11478889  
 
 
Structures of cytochrome c-549 and cytochrome c6 from the cyanobacterium Arthrospira maxima.
M.R.Sawaya, D.W.Krogmann, A.Serag, K.K.Ho, T.O.Yeates, C.A.Kerfeld.
 
  ABSTRACT  
 
Cytochrome c(6) and cytochrome c-549 are small (89 and 130 amino acids, respectively) monoheme cytochromes that function in photosynthesis. They appear to have descended relatively recently from the same ancestral gene but have diverged to carry out very different functional roles, underscored by the large difference between their midpoint potentials of nearly 600 mV. We have determined the X-ray crystal structures of both proteins isolated from the cyanobacterium Arthrospira maxima. The two structures are remarkably similar, superimposing on backbone atoms with an rmsd of 0.7 A. Comparison of the two structures suggests that differences in solvent exposure of the heme and the electrostatic environment of the heme propionates, as well as in heme iron ligation, are the main determinants of midpoint potential in the two proteins. In addition, the crystal packing of both A. maxima cytochrome c-549 and cytochrome c(6) suggests that the proteins oligomerize. Finally, the cytochrome c-549 dimer we observe can be readily fit into the recently described model of cyanobacterial photosystem II.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21267610 B.S.Rajagopal, M.T.Wilson, D.S.Bendall, C.J.Howe, and J.A.Worrall (2011).
Structural and kinetic studies of imidazole binding to two members of the cytochrome c (6) family reveal an important role for a conserved heme pocket residue.
  J Biol Inorg Chem, 16, 577-588.
PDB code: 3ph2
19129656 H.Akazaki, F.Kawai, M.Hosokawa, T.Hama, H.Chida, T.Hirano, B.K.Lim, N.Sakurai, W.Hakamata, S.Y.Park, T.Nishio, and T.Oku (2009).
Crystallization and structural analysis of cytochrome c(6) from the diatom Phaeodactylum tricornutum at 1.5 A resolution.
  Biosci Biotechnol Biochem, 73, 189-191.
PDB code: 3dmi
19678839 W.Bialek, S.Krzywda, M.Jaskolski, and A.Szczepaniak (2009).
Atomic-resolution structure of reduced cyanobacterial cytochrome c6 with an unusual sequence insertion.
  FEBS J, 276, 4426-4436.
PDB code: 3dr0
  18678931 H.Akazaki, F.Kawai, H.Chida, Y.Matsumoto, M.Hirayama, K.Hoshikawa, S.Unzai, W.Hakamata, T.Nishio, S.Y.Park, and T.Oku (2008).
Cloning, expression and purification of cytochrome c(6) from the brown alga Hizikia fusiformis and complete X-ray diffraction analysis of the structure.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 674-680.
PDB code: 2zbo
18716894 I.Enami, A.Okumura, R.Nagao, T.Suzuki, M.Iwai, and J.R.Shen (2008).
Structures and functions of the extrinsic proteins of photosystem II from different species.
  Photosynth Res, 98, 349-363.  
18703839 P.Lukat, M.Hoffmann, and O.Einsle (2008).
Crystal packing of the c(6)-type cytochrome OmcF from Geobacter sulfurreducens is mediated by an N-terminal Strep-tag II.
  Acta Crystallogr D Biol Crystallogr, 64, 919-926.
PDB code: 3dp5
15978038 C.Lange, I.Luque, M.Hervás, J.Ruiz-Sanz, P.L.Mateo, and M.A.De la Rosa (2005).
Role of the surface charges D72 and K8 in the function and structural stability of the cytochrome c from Nostoc sp. PCC 7119.
  FEBS J, 272, 3317-3327.  
14729215 J.De Las Rivas, M.Balsera, and J.Barber (2004).
Evolution of oxygenic photosynthesis: genome-wide analysis of the OEC extrinsic proteins.
  Trends Plant Sci, 9, 18-25.  
15031714 K.Ifuku, T.Nakatsu, H.Kato, and F.Sato (2004).
Crystal structure of the PsbP protein of photosystem II from Nicotiana tabacum.
  EMBO Rep, 5, 362-367.
PDB code: 1v2b
14511373 M.Balsera, J.B.Arellano, F.Pazos, D.Devos, A.Valencia, and J.De Las Rivas (2003).
The single tryptophan of the PsbQ protein of photosystem II is at the end of a 4-alpha-helical bundle domain.
  Eur J Biochem, 270, 3916-3927.  
12518057 N.Kamiya, and J.R.Shen (2003).
Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution.
  Proc Natl Acad Sci U S A, 100, 98.
PDB code: 1izl
12077429 C.A.Kerfeld, M.R.Sawaya, D.W.Krogmann, and T.O.Yeates (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.
PDB code: 1kib
12356767 P.B.Crowley, A.Díaz-Quintana, F.P.Molina-Heredia, P.Nieto, M.Sutter, W.Haehnel, M.A.De La Rosa, and M.Ubbink (2002).
The interactions of cyanobacterial cytochrome c6 and cytochrome f, characterized by NMR.
  J Biol Chem, 277, 48685-48689.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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