3qfu | pdb_00003qfu

Crystal structure of Yeast Hsp70 (Bip/kar2) complexed with ADP

spinqualitylabelsall models 3qfu, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3qfu is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG, PO4 Related: 3qfp, 3qml Gene: KAR2, GRP78, SSD1, YJL034W, J1248 (Saccharomyces cerevisiae) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Sil1 functions as a nucleotide exchange factor (NEF) for Bip in eukaryotic cells. In order to understand how Sil1 functions as a NEF, we analyzed the crystal structure of the yeast Bip-Sil1 complex at a resolution of 2.3A. In the complex, the Sil1 molecule acts as a "molecular clamp" which binds to the IIb lobe of the Bip ATPase domain. Sil1 binding causes lobe IIb to rotate ~13.5 degrees away from the ADP-binding pocket and lobe Ib to rotate in the opposite direction for ~3.7 degrees . These conformational changes in Bip open up the nucleotide-binding pocket in the ATPase domain and simultaneously disrupt the hydrogen bonds between Bip and bound ADP, thus providing a mechanism for ADP release. We also demonstrate that Sil1 mutations that disrupt binding to the Bip ATPase domain abolish Sil1's ability to stimulate Bip ATPase activity. Structural analysis of the Sil1-Bip complex reveals how Sil1 functions as a nucleotide exchange factor.,Yan M, Li J, Sha B Biochem J. 2011 Jun 15. PMID:21675960 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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