Structural genomics of Caenorhabditis elegans: structure of the BAG domain.
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.
Symersky
J
J
Southeast Collaboratory for Structural Genomics, Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Zhang
Y
Y
Schormann
N
N
Li
S
S
Bunzel
R
R
Pruett
P
P
Luan
C H
CH
Luo
M
M
D000818:Animals; D017173:Caenorhabditis elegans / Q000737:chemistry* / Q000235:genetics; D029742:Caenorhabditis elegans Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D019254:Genes, bcl-2 / Q000235:genetics*; D023281:Genomics; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D012371:Robotics; D014961:X-Ray Diffraction
D029742:Caenorhabditis elegans Proteins; D018840:HSP70 Heat-Shock Proteins