3HIP

HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM

3HIP の概要

• エントリーDOI: 10.2210/pdb3hip/pdb
• 分子名称: HIGH-POTENTIAL IRON-SULFUR PROTEIN, IRON/SULFUR CLUSTER (2 entities in total)
• 機能のキーワード: electron transfer, photosynthesis, metalloprotein
• 由来する生物種: Marichromatium purpuratum
• 細胞内の位置: Periplasm: P59860
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 27340.28

構造登録者

Kerfeld, C.A.,Salmeen, A.E.,Yeates, T.O. (登録日: 1998-06-15, 公開日: 1998-11-11, 最終更新日: 2024-05-22)

主引用文献

Kerfeld, C.A.,Salmeen, A.E.,Yeates, T.O.
Crystal structure and possible dimerization of the high-potential iron-sulfur protein from Chromatium purpuratum.
Biochemistry, 37:13911-13917, 1998

PubMed Abstract: The crystal structure of the high-potential iron-sulfur protein (HiPIP) isolated from Chromatium purpuratum is reported at 2.7 A resolution. The three HiPIP molecules in the asymmetric unit of the crystals form one and one-half dimers. Two molecules are related by a noncrystallographic symmetry rotation of approximately 175 degrees with negligible translation along the dyad axis. The third molecule in the asymmetric unit also forms a dimer with a second HiPIP molecule across the crystallographic 2-fold symmetry axis. The Fe4S4 clusters in both the crystallographic and noncrystallographic dimers are separated by approximately 13.0 A. Solution studies give mixed results regarding the oligomeric state of the C. purpuratum HiPIP. A comparison with crystal structures of HiPIPs from other species shows that HiPIP tends to associate rather nonspecifically about a conserved, relatively hydrophobic surface patch to form dimers.

PubMed: 9760225
DOI: 10.1021/bi9810252

実験手法

X-RAY DIFFRACTION (2.8 Å)