TY - JOUR
T1 - Structural genomics of Caenorhabditis elegans
T2 - Structure of the BAG domain
AU - Symersky, J.
AU - Zhang, Y.
AU - Schormann, N.
AU - Li, S.
AU - Bunzel, R.
AU - Pruett, P.
AU - Luan, C. H.
AU - Luo, M.
PY - 2004/9
Y1 - 2004/9
N2 - 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 β-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.
AB - 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 β-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.
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U2 - 10.1107/S0907444904017603
DO - 10.1107/S0907444904017603
M3 - Article
C2 - 15333932
AN - SCOPUS:16644379039
SN - 0907-4449
VL - 60
SP - 1606
EP - 1610
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 9
ER -