1HPI

MOLECULAR STRUCTURE OF THE OXIDIZED HIGH-POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM ECTOTHIORHODOSPIRA VACUOLATA

1HPI の概要

• エントリーDOI: 10.2210/pdb1hpi/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: Ectothiorhodospira shaposhnikovii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8176.22

構造登録者

Benning, M.M.,Meyer, T.E.,Rayment, I.,Holden, H.M. (登録日: 1993-12-09, 公開日: 1994-04-30, 最終更新日: 2024-02-07)

主引用文献

Benning, M.M.,Meyer, T.E.,Rayment, I.,Holden, H.M.
Molecular structure of the oxidized high-potential iron-sulfur protein isolated from Ectothiorhodospira vacuolata.
Biochemistry, 33:2476-2483, 1994

PubMed Abstract: The high-potential iron-sulfur protein (iso-form II) isolated from Ectothiorhodospira vacuolata has been crystallized and its three-dimensional structure determined by molecular replacement procedures and refined to 1.8-A resolution with a crystallographic R factor of 16.3%. Crystals employed in the investigation belonged to the space group C222(1) with unit cell dimensions of a = 58.4 A, b = 64.7 A, and c = 39.3 A and one molecule per asymmetric unit. Like those HiPIPs structurally characterized thus far, the E. vacuolata molecule contains mostly reverse turns that wrap around the iron-sulfur cluster with cysteine residues 34, 37, 51, and 65 ligating the metal center to the polypeptide chain. There are 57 ordered solvent molecules, most of which lie at the surface of the protein. Two of these water molecules play important structural roles by stabilizing the loops located between Asp 42 and Lys 57. The metal center binding pocket is decidedly hydrophobic with the closest solvent molecule being 6.9 A from S2 of the [4Fe-4S] cluster. The E. vacuolata HiPIP molecules pack in the crystalline lattice as dimers with their iron-sulfur centers approximately 17.5 A apart. On the basis of biochemical properties, it was anticipated that the E. vacuolata HiPIP would be structurally more similar to the HiPIP isolated from Ectothiorhodospira halophila than to the protein obtained from Chromatium vinosum. In fact, the E. vacuolata molecule is as structurally close to the C. vinosum HiPIP as it is to the E. halophila protein due to the presence of various insertions and deletions that disrupt local folding.(ABSTRACT TRUNCATED AT 250 WORDS)

PubMed: 8117708
DOI: 10.1021/bi00175a016

実験手法

X-RAY DIFFRACTION (1.8 Å)