1DKZ

THE SUBSTRATE BINDING DOMAIN OF DNAK IN COMPLEX WITH A SUBSTRATE PEPTIDE, DETERMINED FROM TYPE 1 NATIVE CRYSTALS

1DKZ の概要

• エントリーDOI: 10.2210/pdb1dkz/pdb
• 分子名称: SUBSTRATE BINDING DOMAIN OF DNAK, SUBSTRATE PEPTIDE (7 RESIDUES) (3 entities in total)
• 機能のキーワード: dnak, heat shock protein 70 kda (hsp70), complex (molecular chaperone-peptide), complex (molecular chaperone-peptide) complex, complex (molecular chaperone/peptide)
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24593.69

構造登録者

Zhu, X.,Zhao, X.,Burkholder, W.F.,Gragerov, A.,Ogata, C.M.,Gottesman, M.E.,Hendrickson, W.A. (登録日: 1996-06-03, 公開日: 1996-12-07, 最終更新日: 2024-02-07)

主引用文献

Zhu, X.,Zhao, X.,Burkholder, W.F.,Gragerov, A.,Ogata, C.M.,Gottesman, M.E.,Hendrickson, W.A.
Structural analysis of substrate binding by the molecular chaperone DnaK.
Science, 272:1606-1614, 1996

PubMed Abstract: DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote protein folding, interaction, and translocation, both constitutively and in response to stress, by binding to unfolded polypeptide segments. These proteins have two functional units: a substrate-binding portion binds the polypeptide, and an adenosine triphosphatase portion facilitates substrate exchange. The crystal structure of a peptide complex with the substrate-binding unit of DnaK has now been determined at 2.0 angstroms resolution. The structure consists of a beta-sandwich subdomain followed by alpha-helical segments. The peptide is bound to DnaK in an extended conformation through a channel defined by loops from the beta sandwich. An alpha-helical domain stabilizes the complex, but does not contact the peptide directly. This domain is rotated in the molecules of a second crystal lattice, which suggests a model of conformation-dependent substrate binding that features a latch mechanism for maintaining long lifetime complexes.

PubMed: 8658133

実験手法

X-RAY DIFFRACTION (2 Å)