Structural highlights
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 crystal structure of Rhodoferax fermentans high-potential iron protein (HiPIP) has been solved by MAD methods using the anomalous signal from the Fe atoms in the [Fe(4)S(4)] cluster present in the protein and refined to a resolution of 1.45 A. The peptide chain is well defined except in the N- and C-terminal areas. The structure of the protein reveals the presence of three helical fragments, a small beta-sheet and several turns, with the [Fe(4)S(4)] cluster being located close to a surface patch containing several well conserved aromatic residues. The protein fold is very similar to the structures of other known HiPIPs, especially in the region proximal to the [Fe(4)S(4)] cluster, while the largest differences are observed on the opposite side of the protein, which is rich in positive charges and has no sequential homology to other HiPIP families.
Structure of Rhodoferax fermentans high-potential iron-sulfur protein solved by MAD.,Gonzalez A, Benini S, Ciurli S Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1582-8. Epub 2003, Aug 19. PMID:12925788[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gonzalez A, Benini S, Ciurli S. Structure of Rhodoferax fermentans high-potential iron-sulfur protein solved by MAD. Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1582-8. Epub 2003, Aug 19. PMID:12925788
