Structure of Rhodoferax fermentans high-potential iron-sulfur protein solved by MAD.
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.
González
Ana
A
Stanford Synchrotron Radiation Laboratory, 2575 Sand Hill Road MS99, Menlo Park, CA 94025, USA.
Benini
Stefano
S
Ciurli
Stefano
S
D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D016992:Rhodobacter / Q000737:chemistry*; D040681:Structural Homology, Protein
D001426:Bacterial Proteins; D007506:Iron-Sulfur Proteins