1IUA

Ultra-high resolution structure of HiPIP from Thermochromatium tepidum

Summary for 1IUA

• Entry DOI: 10.2210/pdb1iua/pdb
• Related: 1EYT
• Descriptor: High-potential iron-sulfur protein, SULFATE ION, IRON/SULFUR CLUSTER, ... (4 entities in total)
• Functional Keywords: hipip, electron transport
• Biological source: Thermochromatium tepidum
• Total number of polymer chains: 1
• Total formula weight: 9433.68

Authors

Liu, L.,Nogi, T.,Kobayashi, M.,Nozawa, T.,Miki, K. (deposition date: 2002-03-01, release date: 2002-03-20, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (0.8 Å)