3BVO

Crystal structure of human co-chaperone protein HscB

3BVO の概要

• エントリーDOI: 10.2210/pdb3bvo/pdb
• 分子名称: Co-chaperone protein HscB, mitochondrial precursor, ZINC ION, SULFATE ION (3 entities in total)
• 機能のキーワード: co-chaperone protein hscb, structural genomics medical relevance, protein structure initiative, psi-2, center for eukaryotic structural genomics, cesg, mitochondrion, transit peptide, chaperone
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm : Q8IWL3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49022.50

構造登録者

Bitto, E.,Bingman, C.A.,McCoy, J.G.,Wesenberg, G.E.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG) (登録日: 2008-01-07, 公開日: 2008-01-15, 最終更新日: 2024-11-20)

主引用文献

Bitto, E.,Bingman, C.A.,Bittova, L.,Kondrashov, D.A.,Bannen, R.M.,Fox, B.G.,Markley, J.L.,Phillips, G.N.
Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain.
J.Biol.Chem., 283:30184-30192, 2008

PubMed Abstract: Iron-sulfur proteins play indispensable roles in a broad range of biochemical processes. The biogenesis of iron-sulfur proteins is a complex process that has become a subject of extensive research. The final step of iron-sulfur protein assembly involves transfer of an iron-sulfur cluster from a cluster-donor to a cluster-acceptor protein. This process is facilitated by a specialized chaperone system, which consists of a molecular chaperone from the Hsc70 family and a co-chaperone of the J-domain family. The 3.0 A crystal structure of a human mitochondrial J-type co-chaperone HscB revealed an L-shaped protein that resembles Escherichia coli HscB. The important difference between the two homologs is the presence of an auxiliary metal-binding domain at the N terminus of human HscB that coordinates a metal via the tetracysteine consensus motif CWXCX(9-13)FCXXCXXXQ. The domain is found in HscB homologs from animals and plants as well as in magnetotactic bacteria. The metal-binding site of the domain is structurally similar to that of rubredoxin and several zinc finger proteins containing rubredoxin-like knuckles. The normal mode analysis of HscB revealed that this L-shaped protein preferentially undergoes a scissors-like motion that correlates well with the conformational changes of human HscB observed in the crystals.

PubMed: 18713742
DOI: 10.1074/jbc.M804746200

実験手法

X-RAY DIFFRACTION (3 Å)