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PDBsum entry 2gim

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protein metals Protein-protein interface(s) links
Electron transport PDB id
2gim

 

 

 

 

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Contents
Protein chains
106 a.a. *
Metals
_CU ×2
Waters ×315
* Residue conservation analysis
PDB id:
2gim
Name: Electron transport
Title: 1.6 angstrom structure of plastocyanin from anabaena variabilis
Structure: Plastocyanin. Chain: a, c. Engineered: yes
Source: Anabaena variabilis. Organism_taxid: 1172. Gene: pete. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.60Å     R-factor:   0.211     R-free:   0.260
Authors: L.Schmidt,P.Harris,H.E.M.Christensen
Key ref:
L.Schmidt et al. (2006). Structure of plastocyanin from the cyanobacterium Anabaena variabilis. Acta Crystallogr D Biol Crystallogr, 62, 1022-1029. PubMed id: 16929103 DOI: 10.1107/S0907444906023638
Date:
29-Mar-06     Release date:   11-Apr-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0C178  (PLAS_ANAVA) -  Plastocyanin from Anabaena variabilis
Seq:
Struc:
105 a.a.
106 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1107/S0907444906023638 Acta Crystallogr D Biol Crystallogr 62:1022-1029 (2006)
PubMed id: 16929103  
 
 
Structure of plastocyanin from the cyanobacterium Anabaena variabilis.
L.Schmidt, H.E.Christensen, P.Harris.
 
  ABSTRACT  
 
Plastocyanin from the cyanobacterium Anabaena variabilis was heterologously produced in Escherichia coli and purified. Plate-like crystals were obtained by crystallization in 1.15 M trisodium citrate and 7.67 mM sodium borate buffer pH 8.5. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 67.85, b = 45.81, c = 63.41 Angstrom. The structure of the oxidized protein was solved to a resolution of 1.6 Angstrom using plastocyanin from Phormidium laminosum as a search model. Two molecules were found in the asymmetric unit. The electrostatic surface of the basic protein showed a large population of positively charged residues in the northern site, whereas the eastern site lacked the two strongly negatively charged patches. The copper ion was found to be relatively mobile and there were two distinct conformations of His61.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 Superimposed structures of A. variabilis plastocyanin (red and cyan) and poplar plastocyanin (green and grey; PDB code 1plc ; Guss et al., 1992[Guss, J. M., Bartunik, H. D. & Freeman, H. C. (1992). Acta Cryst. B48, 790-811.]). The structures are represented by the C^ atoms and the Cu ions. 58-61 refer to the residues Ser58-Asp61 in poplar plastocyanin. The figure was prepared using CCP4mg (Potterton et al., 2002[Potterton, E., McNicholas, S., Krissinel, E., Cowtan, K. & Noble, M. (2002). Acta Cryst. D58, 1955-1957.]).
Figure 5.
Figure 5 2F[obs] - F[calc] [A]-weighted electron-density map showing the hydrogen-bonding networks of the two conformations of His61 in A. variabilis chains A (left) and C (right). The higher occupied (occupancy 0.55 in chain A and 0.65 in chain C) conformations are shown in green (C-atom colour) and the lower occupied (0.45 in chain A and 0.35 in chain C) are shown in light blue. This figure was produced using PyMOL (DeLano, 2002[DeLano, W. L. (2002). The PyMOL Molecular Visualization System. DeLano Scientific, San Carlos, CA, USA. http://www.pymol.org .]).
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 1022-1029) copyright 2006.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18214953 M.A.Hass, M.R.Jensen, and J.J.Led (2008).
Probing electric fields in proteins in solution by NMR spectroscopy.
  Proteins, 72, 333-343.  
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.

 

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