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PDBsum entry 1ewh
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protein ligands Protein-protein interface(s) links
Electron transport PDB id
1ewh

 

 

 

 

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Contents
Protein chains
251 a.a. *
Ligands
HEC ×3
ACT
Waters ×721
* Residue conservation analysis
PDB id:
1ewh
Name: Electron transport
Title: Structure of cytochrome f from chlamydomonas reinhardtii
Structure: Cytochrome f. Chain: a, b, c. Fragment: n-terminal soluble fragment. Engineered: yes
Source: Chlamydomonas reinhardtii. Organism_taxid: 3055. Cellular_location: chloroplast. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.35Å     R-factor:   0.187     R-free:   0.256
Authors: G.Sainz,C.J.Carrell,M.V.Ponamarev,G.M.Soriano,W.A.Cramer,J.L.Smith
Key ref:
G.Sainz et al. (2000). Interruption of the internal water chain of cytochrome f impairs photosynthetic function. Biochemistry, 39, 9164-9173. PubMed id: 10924110 DOI: 10.1021/bi0004596
Date:
25-Apr-00     Release date:   09-Aug-00    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P23577  (CYF_CHLRE) -  Cytochrome f from Chlamydomonas reinhardtii
Seq:
Struc: 		317 a.a.
251 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1021/bi0004596 Biochemistry 39:9164-9173 (2000)
PubMed id: 10924110  
 
 
Interruption of the internal water chain of cytochrome f impairs photosynthetic function.
G.Sainz, C.J.Carrell, M.V.Ponamarev, G.M.Soriano, W.A.Cramer, J.L.Smith.
 
  ABSTRACT  
 
The structure of cytochrome f includes an internal chain of five water molecules and six hydrogen-bonding side chains, which are conserved throughout the phylogenetic range of photosynthetic organisms from higher plants, algae, and cyanobacteria. The in vivo electron transfer capability of Chlamydomonas reinhardtii cytochrome f was impaired in site-directed mutants of the conserved Asn and Gln residues that form hydrogen bonds with water molecules of the internal chain [Ponamarev, M. V., and Cramer, W. A. (1998) Biochemistry 37, 17199-17208]. The 251-residue extrinsic functional domain of C. reinhardtii cytochrome f was expressed in Escherichia coli without the 35 C-terminal residues of the intact cytochrome that contain the membrane anchor. Crystal structures were determined for the wild type and three "water chain" mutants (N168F, Q158L, and N153Q) having impaired photosynthetic and electron transfer function. The mutant cytochromes were produced, folded, and assembled heme at levels identical to that of the wild type in the E. coli expression system. N168F, which had a non-photosynthetic phenotype and was thus most affected by mutational substitution, also had the greatest structural perturbation with two water molecules (W4 and W5) displaced from the internal chain. Q158L, the photosynthetic mutant with the largest impairment of in vivo electron transfer, had a more weakly bound water at one position (W1). N153Q, a less impaired photosynthetic mutant, had an internal water chain with positions and hydrogen bonds identical to those of the wild type. The structure data imply that the waters of the internal chain, in addition to the surrounding protein, have a significant role in cytochrome f function.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20672171 K.A.Lukyanov, E.O.Serebrovskaya, S.Lukyanov, and D.M.Chudakov (2010).
Fluorescent proteins as light-inducible photochemical partners.
  Photochem Photobiol Sci, 9, 1301-1306.  
19773387 A.Zuppini, C.Gerotto, R.Moscatiello, E.Bergantino, and B.Baldan (2009).
Chlorella saccharophila cytochrome f and its involvement in the heat shock response.
  J Exp Bot, 60, 4189-4200.  
19737938 S.Pletnev, N.G.Gurskaya, N.V.Pletneva, K.A.Lukyanov, D.M.Chudakov, V.I.Martynov, V.O.Popov, M.V.Kovalchuk, A.Wlodawer, Z.Dauter, and V.Pletnev (2009).
Structural basis for phototoxicity of the genetically encoded photosensitizer KillerRed.
  J Biol Chem, 284, 32028-32039.
PDB codes: 3gb3 3gl4
16239335 E.J.Haddadian, and E.L.Gross (2006).
A Brownian dynamics study of the effects of cytochrome f structure and deletion of its small domain in interactions with cytochrome c6 and plastocyanin in Chlamydomonas reinhardtii.
  Biophys J, 90, 566-577.  
16756511 W.A.Cramer, H.Zhang, J.Yan, G.Kurisu, and J.L.Smith (2006).
Transmembrane traffic in the cytochrome b6f complex.
  Annu Rev Biochem, 75, 769-790.  
15691836 F.Musiani, A.Dikiy, A.Y.Semenov, and S.Ciurli (2005).
Structure of the intermolecular complex between plastocyanin and cytochrome f from spinach.
  J Biol Chem, 280, 18833-18841.
PDB code: 1ylb
15313237 J.L.Smith, H.Zhang, J.Yan, G.Kurisu, and W.A.Cramer (2004).
Cytochrome bc complexes: a common core of structure and function surrounded by diversity in the outlying provinces.
  Curr Opin Struct Biol, 14, 432-439.  
15267612 V.Zoete, and M.Meuwly (2004).
On the influence of semirigid environments on proton transfer along molecular chains.
  J Chem Phys, 120, 7085-7094.  
14647374 D.Stroebel, Y.Choquet, J.L.Popot, and D.Picot (2003).
An atypical haem in the cytochrome b(6)f complex.
  Nature, 426, 413-418.
PDB code: 1q90
14526088 G.Kurisu, H.Zhang, J.L.Smith, and W.A.Cramer (2003).
Structure of the cytochrome b6f complex of oxygenic photosynthesis: tuning the cavity.
  Science, 302, 1009-1014.
PDB codes: 1um3 1vf5
12207018 G.M.Soriano, L.W.Guo, C.De Vitry, T.Kallas, and W.A.Cramer (2002).
Electron transfer from the Rieske iron-sulfur protein (ISP) to cytochrome f in vitro. Is a guided trajectory of the ISP necessary for competent docking?
  J Biol Chem, 277, 41865-41871.  
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 codes are shown on the right.

 

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