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PDBsum entry 2v8a

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protein ligands Protein-protein interface(s) links
Electron transport PDB id
2v8a

 

 

 

 

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Contents
Protein chains
160 a.a. *
161 a.a. *
Ligands
CYC ×2
* Residue conservation analysis
PDB id:
2v8a
Name: Electron transport
Title: The structure of thermosynechococcus elongatus allophycocyanin at 3.5 angstroems.
Structure: Allophycocyanin alpha chain. Chain: a. Allophycocyanin beta chain. Chain: b
Source: Thermosynechococcus elongatus. Organism_taxid: 197221. Strain: bp-1. Strain: bp-1
Resolution:
3.50Å     R-factor:   0.261     R-free:   0.285
Authors: J.W.Murray,K.Maghlaoui,J.Barber
Key ref: J.W.Murray et al. (2007). The structure of allophycocyanin from Thermosynechococcus elongatus at 3.5 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 998. PubMed id: 18084078
Date:
06-Aug-07     Release date:   11-Dec-07    
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P50030  (PHAA_THEEB) -  Allophycocyanin alpha chain from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
Seq:
Struc:
161 a.a.
160 a.a.
Protein chain
Pfam   ArchSchema ?
P50031  (APCB_THEEB) -  Allophycocyanin beta chain from Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
Seq:
Struc:
161 a.a.
161 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
Acta Crystallogr Sect F Struct Biol Cryst Commun 63:998 (2007)
PubMed id: 18084078  
 
 
The structure of allophycocyanin from Thermosynechococcus elongatus at 3.5 A resolution.
J.W.Murray, K.Maghlaoui, J.Barber.
 
  ABSTRACT  
 
Cyanobacteria and red algae use light-harvesting pigments bound by proteins to capture solar radiation and to channel excitation energy into their reaction centres. In most cyanobacteria, a multi-megadalton soluble structure known as the phycobilisome is a major light-harvesting system. Allophycocyanin is the main component of the phycobilisome core, forming a link between the rest of the phycobilisome and the reaction-centre core. The crystal structure of allophycocyanin from Thermosynechococcus elongatus (TeAPC) has been determined and refined at 3.5 A resolution to a crystallographic R value of 26.0% (R(free) = 28.5%). The structure was solved by molecular replacement using the allophycocyanin structure from Spirulina platensis as the search model. The asymmetric unit contains an (alphabeta) monomer which is expanded by symmetry to a crystallographic trimer.
 

 

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