1ISU

THE THREE-DIMENSIONAL STRUCTURE OF THE HIGH-POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM THE PURPLE PHOTOTROPHIC BACTERIUM RHODOCYCLUS TENUIS DETERMINED AND REFINED AT 1.5 ANGSTROMS RESOLUTION

1ISU の概要

• エントリーDOI: 10.2210/pdb1isu/pdb
• 分子名称: HIGH POTENTIAL IRON SULFUR PROTEIN, IRON/SULFUR CLUSTER (3 entities in total)
• 機能のキーワード: electron transfer(iron-sulfur protein)
• 由来する生物種: Rhodocyclus tenuis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13311.68

構造登録者

Holden, H.M. (登録日: 1992-09-09, 公開日: 1994-01-31, 最終更新日: 2024-02-07)

主引用文献

Rayment, I.,Wesenberg, G.,Meyer, T.E.,Cusanovich, M.A.,Holden, H.M.
Three-dimensional structure of the high-potential iron-sulfur protein isolated from the purple phototrophic bacterium Rhodocyclus tenuis determined and refined at 1.5 A resolution.
J.Mol.Biol., 228:672-686, 1992

PubMed Abstract: The molecular structure of the high-potential iron-sulfur protein (HiPIP) isolated from the phototrophic bacterium, Rhodocyclus tenuis, has been solved and refined to a nominal resolution of 1.5 A with a crystallographic R-factor of 17.3% for all measured X-ray data from 30 A to 1.5 A. It is the smallest of the HiPIP structures studied thus far with 62 amino acid residues. Crystals used in the investigation belonged to the space group P2(1) with unit cell dimensions of a = 36.7 A, b = 52.6 A, c = 27.6 A and beta = 90.8 degrees and contained two molecules per asymmetric unit. The structure was solved by a combination of multiple isomorphous replacement with two heavy-atom derivatives, anomalous scattering from the iron-sulfur cluster, symmetry averaging and solvent flattening. The folding motif for this HiPIP is characterized by one small alpha-helix, six Type I turns, an approximate Type II turn and one Type I' turn. As in other HiPIPs, the iron-sulfur cluster is co-ordinated by four cysteinyl ligands and exhibits a cubane-like motif. These cysteinyl ligands are all located in Type I turns. The hydrogen bonding around the metal cluster in the R. tenuis protein is similar to the patterns observed in the Chromatium vinosum and Ectothiorhodospira halophila HiPIPs. Several of the amino acid residues invariant in the previously determined C. vinosum and E. halophila structures are not retained in the R. tenuis molecule. There are 13 solvent molecules structurally conserved between the two R. tenuis HiPIP molecules in the asymmetric unit, some of which are important for stabilizing surface loops. Interestingly, while it is assumed that this HiPIP functions as a monomer in solution, the two molecules in the asymmetric unit pack as a dimer and are related to each other by an approximate twofold rotation axis.

PubMed: 1453470
DOI: 10.1016/0022-2836(92)90849-F

実験手法

X-RAY DIFFRACTION (1.5 Å)