Summary: Apocytochrome F, C-terminal
This is the Wikipedia entry entitled "Cytochrome f". More...
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Cytochrome f Edit Wikipedia article
|cytochrome f from the b6f complex of phormidium laminosum|
Cytochrome f is the largest subunit of cytochrome b6f complex (plastoquinol—plastocyanin reductase; EC 184.108.40.206). In its structure and functions, the cytochrome b6f complex bears extensive analogy to the cytochrome bc1 complex of mitochondria and photosynthetic purple bacteria. Cytochrome f (cyt f) plays a role analogous to that of cytochrome c1, in spite of their different structures.
The 3D structure of Brassica rapa (Turnip) cyt f has been determined. The lumen-side segment of cyt f includes two structural domains: a small one above a larger one that, in turn, is on top of the attachment to the membrane domain. The large domain consists of an anti-parallel beta-sandwich and a short haem-binding peptide, which form a three-layer structure. The small domain is inserted between beta-strands F and G of the large domain and is an all-beta domain. The haem nestles between two short helices at the N terminus of cyt f. Within the second helix is the sequence motif for the c-type cytochromes, CxxCH (residues 21-25), which is covalently attached to the haem through thioether bonds to Cys-21 and Cys-24. His-25 is the fifth haem iron ligand. The sixth haem iron ligand is the alpha-amino group of Tyr-1 in the first helix. Cyt f has an internal network of water molecules that may function as a proton wire. The water chain appears to be a conserved feature of cyt f.
- Prince RC, George GN (June 1995). "Cytochrome f revealed". Trends Biochem. Sci. 20 (6): 217–8. PMID 7631417.
- Martinez SE, Huang D, Ponomarev M, Cramer WA, Smith JL (June 1996). "The heme redox center of chloroplast cytochrome f is linked to a buried five-water chain". Protein Sci. 5 (6): 1081–92. doi:10.1002/pro.5560050610. PMC 2143431. PMID 8762139. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2143431/.
 Further reading
- Bendall, D.S. (2004). "The unfinished story of cytochrome f". Photosynth. Res. 80 (1–3): 265–276. doi:10.1023/B:PRES.0000030454.23940.f9. PMID 16328825.
- Cramer, W.A., Martinez, S.E., Huang, D., Tae, G.S., Everly, R.M., Heymann, J.B., Cheng, R.H., Baker, T.S. and Smith, J.L. (1994). "Structural aspects of the cytochrome b6f complex; structure of the lumen-side domain of cytochrome f". J. Bioenerg. Biomembr. 26 (1): 31–47. doi:10.1007/BF00763218. PMID 8027021.
Apocytochrome F, C-terminal Provide feedback
This is a sub-family of cytochrome C. See PF00034.
Martinez SE, Huang D, Szczepaniak A, Cramer WA, Smith JL; , Structure 1994;2:95-105.: Crystal structure of chloroplast cytochrome f reveals a novel cytochrome fold and unexpected heme ligation. PUBMED:8081747 EPMC:8081747
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002325
The cytochrome b6f integral membrane protein complex transfers electrons between the two reaction centre complexes of oxygenic photosynthetic membranes, and participates in formation of the transmembrane electrochemical proton gradient by also transferring protons from the stromal to the internal lumen compartment [PUBMED:]. The cytochrome b6f complex contains four polypeptides: cytochrome f (285 aa); cytochrome b6 (215 aa); Rieske iron-sulphur protein (179 aa); and subunit IV (160 aa) [PUBMED:8027021]. In its structure and functions, the cytochrome b6f complex bears extensive analogy to the cytochrome bc1 complex of mitochondria and photosynthetic purple bacteria; cytochrome f (cyt f) plays a role analogous to that of cytochrome c1, in spite of their different structures [PUBMED:7631417].
|Cellular component||integral to thylakoid membrane (GO:0031361)|
|Molecular function||electron carrier activity (GO:0009055)|
|heme binding (GO:0020037)|
|iron ion binding (GO:0005506)|
|Biological process||photosynthesis (GO:0015979)|
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This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
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Curation and family details
|Seed source:||Pfam-B_1294 (release 3.0)|
|Author:||Finn RD, Bateman A|
|Number in seed:||49|
|Number in full:||697|
|Average length of the domain:||114.80 aa|
|Average identity of full alignment:||74 %|
|Average coverage of the sequence by the domain:||37.15 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Apocytochr_F_C domain has been found. There are 30 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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