1T7S

Structural Genomics of Caenorhabditis elegans: Structure of BAG-1 protein

Summary for 1T7S

• Entry DOI: 10.2210/pdb1t7s/pdb
• Related: 1HX1 1I6Z
• Descriptor: BAG-1 cochaperone (2 entities in total)
• Functional Keywords: structural genomics, bag-1 cochaperone, psi, protein structure initiative, southeast collaboratory for structural genomics, secsg, chaperone
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 2
• Total formula weight: 32295.33

Authors

Symersky, J.,Zhang, Y.,Schormann, N.,Li, S.,Bunzel, R.,Pruett, P.,Luan, C.-H.,Luo, M.,Southeast Collaboratory for Structural Genomics (SECSG) (deposition date: 2004-05-10, release date: 2004-05-18, Last modification date: 2024-11-06)

Primary citation

Symersky, J.,Zhang, Y.,Schormann, N.,Li, S.,Bunzel, R.,Pruett, P.,Luan, C.H.,Luo, M.
Structural genomics of Caenorhabditis elegans: structure of the BAG domain.
Acta Crystallogr.,Sect.D, 60:1606-1610, 2004

PubMed Abstract: Binding of the BAG domain to the eukaryotic chaperone heat-shock protein (Hsp70) promotes ATP-dependent release of the protein substrate from Hsp70. Although the murine and human BAG domains have been shown to form an antiparallel three-helix bundle, the Caenorhabditis elegans BAG domain is formed by two antiparallel helices, while the third helix is extended away and stabilized by crystal-packing interactions. A small beta-sheet between helices 2 and 3 interferes with formation of the intramolecular three-helix bundle. However, intermolecular three-helix bundles are observed throughout the crystal packing and suggest that stable functional dimers and tetramers can be formed in solution. The structure may represent a new folding type of the BAG domain.

PubMed: 15333932
DOI: 10.1107/S0907444904017603

Experimental method

X-RAY DIFFRACTION (2.8 Å)