1HLQ

CRYSTAL STRUCTURE OF RHODOFERAX FERMENTANS HIGH POTENTIAL IRON-SULFUR PROTEIN REFINED TO 1.45 A

Summary for 1HLQ

• Entry DOI: 10.2210/pdb1hlq/pdb
• Descriptor: HIGH-POTENTIAL IRON-SULFUR PROTEIN, SULFATE ION, IRON/SULFUR CLUSTER, ... (4 entities in total)
• Functional Keywords: iron sulfur cluster, electron transport
• Biological source: Rhodoferax fermentans
• Total number of polymer chains: 3
• Total formula weight: 25118.14

Authors

Gonzalez, A.,Ciurli, S.,Benini, S. (deposition date: 2000-12-01, release date: 2003-06-03, Last modification date: 2024-02-07)

Primary citation

Gonzalez, A.,Benini, S.,Ciurli, S.
Structure of Rhodoferax fermentans high-potential iron-sulfur protein solved by MAD.
Acta Crystallogr.,Sect.D, 59:1582-1588, 2003

PubMed Abstract: 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.

PubMed: 12925788
DOI: 10.1107/S0907444903014604

Experimental method

X-RAY DIFFRACTION (1.45 Å)