Structural highlights
Function
[AURB_CHLAA] Probably a soluble electron acceptor for the integral membrane protein electron transfer alternative complex III (ACIII).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Auracyanin B structure in space group P6(5).,Lee M, Maher MJ, Freeman HC, Guss JM Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1545-50. Epub 2003, Aug 19. PMID:12925783[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McManus JD, Brune DC, Han J, Sanders-Loehr J, Meyer TE, Cusanovich MA, Tollin G, Blankenship RE. Isolation, characterization, and amino acid sequences of auracyanins, blue copper proteins from the green photosynthetic bacterium Chloroflexus aurantiacus. J Biol Chem. 1992 Apr 5;267(10):6531-40. PMID:1313011
- ↑ Lee M, Maher MJ, Freeman HC, Guss JM. Auracyanin B structure in space group P6(5). Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1545-50. Epub 2003, Aug 19. PMID:12925783
