1IUA

Ultra-high resolution structure of HiPIP from Thermochromatium tepidum

1IUA の概要

• エントリーDOI: 10.2210/pdb1iua/pdb
• 関連するPDBエントリー: 1EYT
• 分子名称: High-potential iron-sulfur protein, SULFATE ION, IRON/SULFUR CLUSTER, ... (4 entities in total)
• 機能のキーワード: hipip, electron transport
• 由来する生物種: Thermochromatium tepidum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9433.68

構造登録者

Liu, L.,Nogi, T.,Kobayashi, M.,Nozawa, T.,Miki, K. (登録日: 2002-03-01, 公開日: 2002-03-20, 最終更新日: 2023-12-27)

主引用文献

Liu, L.,Nogi, T.,Kobayashi, M.,Nozawa, T.,Miki, K.
Ultrahigh-resolution structure of high-potential iron-sulfur protein from Thermochromatium tepidum.
Acta Crystallogr.,Sect.D, 58:1085-1091, 2002

PubMed Abstract: Crystals of the high-potential iron-sulfur protein (HiPIP) from Thermochromatium tepidum diffract X-rays to 0.80 A using synchrotron radiation at 100 K. The crystal structure of this HiPIP was refined at this ultrahigh resolution with anisotropic temperature factors for all atoms to conventional crystallographic R factors of 0.092 and 0.101 for F(o) > 4sigma(F(o)) and all reflections, respectively. The present structure provides a more precise picture than the previous 1.5 A structure and allows location of the positions of most H atoms. The structure revealed a partly hydrophobic cavity near the main hydrophobic area and a much larger inter-cluster approach distance (23.454 A, the c constant of the unit cell) in the crystal packing than other types of HiPIPs. The structural features involved in the electron-transfer reaction of HiPIP are discussed.

PubMed: 12077426
DOI: 10.1107/S0907444902006261

実験手法

X-RAY DIFFRACTION (0.8 Å)