3BVO

Crystal structure of human co-chaperone protein HscB

Summary for 3BVO

• Entry DOI: 10.2210/pdb3bvo/pdb
• Descriptor: Co-chaperone protein HscB, mitochondrial precursor, ZINC ION, SULFATE ION (3 entities in total)
• Functional Keywords: co-chaperone protein hscb, structural genomics medical relevance, protein structure initiative, psi-2, center for eukaryotic structural genomics, cesg, mitochondrion, transit peptide, chaperone
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm : Q8IWL3
• Total number of polymer chains: 2
• Total formula weight: 49022.50

Authors

Bitto, E.,Bingman, C.A.,McCoy, J.G.,Wesenberg, G.E.,Phillips Jr., G.N.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2008-01-07, release date: 2008-01-15, Last modification date: 2024-11-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3 Å)