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PDBsum entry 1ov8

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protein ligands metals Protein-protein interface(s) links
Electron transport PDB id
1ov8
Jmol
Contents
Protein chains
139 a.a. *
Ligands
SO4 ×5
Metals
_CU ×4
_CL ×2
Waters ×559
* Residue conservation analysis
PDB id:
1ov8
Name: Electron transport
Title: Auracyanin b structure in space group, p65
Structure: Auracyanin b. Chain: a, b, c, d. Fragment: n-terminal soluble domain. Synonym: ac-b
Source: Chloroflexus aurantiacus. Organism_taxid: 1108. Other_details: thermophilic green photosynthetic bacterium
Resolution:
1.90Å     R-factor:   0.193     R-free:   0.219
Authors: M.Lee,M.J.Maher,H.C.Freeman,J.M.Guss
Key ref:
M.Lee et al. (2003). Auracyanin B structure in space group P6(5). Acta Crystallogr D Biol Crystallogr, 59, 1545-1550. PubMed id: 12925783 DOI: 10.1107/S0907444903014161
Date:
25-Mar-03     Release date:   09-Sep-03    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P27197  (AURB_CHLAA) -  Auracyanin-B
Seq:
Struc:
235 a.a.
139 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     electron carrier activity     2 terms  

 

 
DOI no: 10.1107/S0907444903014161 Acta Crystallogr D Biol Crystallogr 59:1545-1550 (2003)
PubMed id: 12925783  
 
 
Auracyanin B structure in space group P6(5).
M.Lee, M.J.Maher, H.C.Freeman, J.M.Guss.
 
  ABSTRACT  
 
The structure of auracyanin B, a 'blue' copper protein produced by Chloroflexus aurantiacus, has previously been solved and refined in the hexagonal space group P6(4)22 with a single molecule in the asymmetric unit. The protein has now been crystallized in space group P6(5), with unit-cell parameters a = b = 115.9, c = 108.2 A. In the new crystal form, the asymmetric unit contains four protein molecules. The structure has been solved by molecular replacement and refined at 1.9 A resolution. The final residuals are R = 19.2% and R(free) = 21.9%. In relation to the earlier crystal structure, the doubling of the unit-cell volume and the lower symmetry are explained by small rotations of the molecules with respect to one another.
 
  Selected figure(s)  
 
Figure 3.
Figure 3 Details of a second contact region between molecules, illustrating the deviation from exact crystallographic symmetry. The top panel shows the contact between molecule A (yellow) and C (red) transformed by the symmetry operation (y, 1 + y - x, 7/6 + z). The lower panel shows the equivalent contact between molecules D (blue) and B (green) transformed by the symmetry operation (y, 1 + y - x, 1/6 + z). Since these contacts do not involve molecules related by crystallographic symmetry, the reverse contacts are similar but not identical (Table 4-). The right-hand molecule in the lower panel is displaced downwards in comparison with the upper panel, resulting in the loss of the hydrogen bonds (dotted).
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 1545-1550) copyright 2003.  
  Figure was selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19190939 M.Lee, M.C.del Rosario, H.H.Harris, R.E.Blankenship, J.M.Guss, and H.C.Freeman (2009).
The crystal structure of auracyanin A at 1.85 A resolution: the structures and functions of auracyanins A and B, two almost identical "blue" copper proteins, in the photosynthetic bacterium Chloroflexus aurantiacus.
  J Biol Inorg Chem, 14, 329-345.  
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