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PDBsum entry 1e29

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protein ligands metals links
Electron transport PDB id
1e29

 

 

 

 

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Contents
Protein chain
135 a.a. *
Ligands
HEC
Metals
_CA ×3
Waters ×223
* Residue conservation analysis
PDB id:
1e29
Name: Electron transport
Title: Psii associated cytochrome c549 from synechocystis sp.
Structure: Cytochrome c549. Chain: a
Source: Synechocystis sp. Organism_taxid: 1143. Strain: pcc 6803
Resolution:
1.21Å     R-factor:   0.153     R-free:   0.212
Authors: C.Frazao,F.J.Enguita,R.Coelho,G.M.Sheldrick
Key ref: C.Frazão et al. (2001). Crystal structure of low-potential cytochrome c549 from Synechocystis sp. PCC 6803 at 1.21 A resolution. J Biol Inorg Chem, 6, 324-332. PubMed id: 11315568
Date:
19-May-00     Release date:   04-May-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Q55013  (CY550_SYNY3) -  Photosystem II extrinsic protein V from Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Seq:
Struc:
160 a.a.
135 a.a.
Key:    Secondary structure  CATH domain

 

 
J Biol Inorg Chem 6:324-332 (2001)
PubMed id: 11315568  
 
 
Crystal structure of low-potential cytochrome c549 from Synechocystis sp. PCC 6803 at 1.21 A resolution.
C.Frazão, F.J.Enguita, R.Coelho, G.M.Sheldrick, J.A.Navarro, M.Hervás, M.A.De la Rosa, M.A.Carrondo.
 
  ABSTRACT  
 
The crystal structure of low-potential cytochrome c549, an extrinsic component of the photosystem II (PS II) from Synechocystis sp. PCC 6803, was obtained directly from single-wavelength 1.21 A resolution diffraction data. This is the first monodomain bis-histidinyl monoheme cytochrome c to be structurally characterized. The extended N-terminal region of c549 builds up a two-strand antiparallel beta-sheet in a hairpin motif, which extends through two molecules owing to crystal packing. Both peptide termini are involved in crystal contacts, which may explain their protrusion out of the globular fold. The C-terminus is preceded by a 9 A-long hydrophobic finger extending from a positively charged base and could be involved in PSII interactions, as well as a protruding negative patch built by a set of conserved acidic residues among c549 sequences.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.  
16341897 F.J.Enguita, E.Pohl, D.L.Turner, H.Santos, and M.A.Carrondo (2006).
Structural evidence for a proton transfer pathway coupled with haem reduction of cytochrome c" from Methylophilus methylotrophus.
  J Biol Inorg Chem, 11, 189-196.
PDB codes: 1gu2 1oae
16723351 Y.Kashino, N.Inoue-Kashino, J.L.Roose, and H.B.Pakrasi (2006).
Absence of the PsbQ protein results in destabilization of the PsbV protein and decreased oxygen evolution activity in cyanobacterial photosystem II.
  J Biol Chem, 281, 20834-20841.  
15858265 R.Caliandro, B.Carrozzini, G.L.Cascarano, L.De Caro, C.Giacovazzo, and D.Siliqi (2005).
Phasing at resolution higher than the experimental resolution.
  Acta Crystallogr D Biol Crystallogr, 61, 556-565.  
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
12876351 K.Ifuku, T.Nakatsu, H.Kato, and F.Sato (2003).
Crystallization and preliminary crystallographic studies on the extrinsic 23 kDa protein in the oxygen-evolving complex of photosystem II.
  Acta Crystallogr D Biol Crystallogr, 59, 1462-1463.  
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.  
11815610 J.Nield, M.Balsera, J.De Las Rivas, and J.Barber (2002).
Three-dimensional electron cryo-microscopy study of the extrinsic domains of the oxygen-evolving complex of spinach: assignment of the PsbO protein.
  J Biol Chem, 277, 15006-15012.  
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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