1iua
From Proteopedia
|
Ultra-high resolution structure of HiPIP from Thermochromatium tepidum
Overview
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.
About this Structure
1IUA is a Single protein structure of sequence from Thermochromatium tepidum with and as ligands. Full crystallographic information is available from OCA.
Reference
Ultrahigh-resolution structure of high-potential iron-sulfur protein from Thermochromatium tepidum., Liu L, Nogi T, Kobayashi M, Nozawa T, Miki K, Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1085-91. Epub 2002, Jun 20. PMID:12077426
Page seeded by OCA on Thu Feb 21 13:15:41 2008
