1DKG

CRYSTAL STRUCTURE OF THE NUCLEOTIDE EXCHANGE FACTOR GRPE BOUND TO THE ATPASE DOMAIN OF THE MOLECULAR CHAPERONE DNAK

1DKG の概要

• エントリーDOI: 10.2210/pdb1dkg/pdb
• 分子名称: NUCLEOTIDE EXCHANGE FACTOR GRPE, MOLECULAR CHAPERONE DNAK (3 entities in total)
• 機能のキーワード: hsp70, grpe, molecular chaperone, nucleotide exchange factor, coiled-coil, complex (hsp24-hsp70), complex (hsp24-hsp70) complex, complex (hsp24/hsp70)
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Cytoplasm (Probable): P09372; Cytoplasm: P04475
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 85337.81

構造登録者

Harrison, C.J.,Kuriyan, J. (登録日: 1997-02-13, 公開日: 1997-08-20, 最終更新日: 2024-02-07)

主引用文献

Harrison, C.J.,Hayer-Hartl, M.,Di Liberto, M.,Hartl, F.,Kuriyan, J.
Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK.
Science, 276:431-435, 1997

PubMed Abstract: The crystal structure of the adenine nucleotide exchange factor GrpE in complex with the adenosine triphosphatase (ATPase) domain of Escherichia coli DnaK [heat shock protein 70 (Hsp70)] was determined at 2.8 angstrom resolution. A dimer of GrpE binds asymmetrically to a single molecule of DnaK. The structure of the nucleotide-free ATPase domain in complex with GrpE resembles closely that of the nucleotide-bound mammalian Hsp70 homolog, except for an outward rotation of one of the subdomains of the protein. This conformational change is not consistent with tight nucleotide binding. Two long alpha helices extend away from the GrpE dimer and suggest a role for GrpE in peptide release from DnaK.

PubMed: 9103205
DOI: 10.1126/science.276.5311.431

実験手法

X-RAY DIFFRACTION (2.8 Å)