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2IOQ

Crystal Structure of full-length HTPG, the Escherichia coli HSP90

2IOQ の概要
エントリーDOI10.2210/pdb2ioq/pdb
関連するPDBエントリー1Y4S 1Y4U 2IOP 2IOR
分子名称Chaperone protein htpG (1 entity in total)
機能のキーワードheat shock protein, chaperone, hsp90
由来する生物種Escherichia coli
細胞内の位置Cytoplasm: P0A6Z3
タンパク質・核酸の鎖数2
化学式量合計143038.84
構造登録者
Shiau, A.K.,Harris, S.F.,Agard, D.A. (登録日: 2006-10-10, 公開日: 2006-11-21, 最終更新日: 2024-02-21)
主引用文献Shiau, A.K.,Harris, S.F.,Southworth, D.R.,Agard, D.A.
Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements.
Cell(Cambridge,Mass.), 127:329-340, 2006
Cited by
PubMed Abstract: In eukaryotes, the ubiquitous and abundant members of the 90 kilodalton heat-shock protein (hsp90) chaperone family facilitate the folding and conformational changes of a broad array of proteins important in cell signaling, proliferation, and survival. Here we describe the effects of nucleotides on the structure of full-length HtpG, the Escherichia coli hsp90 ortholog. By electron microscopy, the nucleotide-free, AMPPNP bound, and ADP bound states of HtpG adopt completely distinct conformations. Structural characterization of nucleotide-free and ADP bound HtpG was extended to higher resolution by X-ray crystallography. In the absence of nucleotide, HtpG exhibits an "open" conformation in which the three domains of each monomer present hydrophobic elements into the large cleft formed by the dimer. By contrast, ADP binding drives dramatic conformational changes that allow these hydrophobic elements to converge and shield each other from solvent, suggesting a mechanism by which nucleotides could control client protein binding and release.
PubMed: 17055434
DOI: 10.1016/j.cell.2006.09.027
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.5 Å)
構造検証レポート
Validation report summary of 2ioq
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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