1IM2

HslU, Haemophilus Influenzae, Selenomethionine Variant

1IM2 の概要

• エントリーDOI: 10.2210/pdb1im2/pdb
• 関連するPDBエントリー: 1DO0 1DO2 1G41
• 分子名称: ATP-DEPENDENT HSL PROTEASE ATP-BINDING SUBUNIT HSLU, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: chaperone, aaa family
• 由来する生物種: Haemophilus influenzae
• 細胞内の位置: Cytoplasm (By similarity): P43773
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50668.19

構造登録者

Trame, C.B.,McKay, D.B. (登録日: 2001-05-09, 公開日: 2001-08-08, 最終更新日: 2024-10-30)

主引用文献

Trame, C.B.,McKay, D.B.
Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning.
Acta Crystallogr.,Sect.D, 57:1079-1090, 2001

PubMed Abstract: The structure of the Haemophilus influenzae HslU protein, a molecular chaperone of the Clp/Hsp100 family, has been solved to 2.3 A by molecular replacement using a model of the homologous Escherichia coli protein. The crystals in which the structure was solved have an unusual twinning, or one-dimensional disorder, in which each successive crystal-packing layer is displaced laterally relative to the one below it. A model for the twinning and an algorithm for detwinning the data are described. It is known from other work that when the HslU hexamer binds its cognate protease HslV, the carboxy-terminal helices of HslU protomers distend and bind between HslV subunits. Comparison of HslU alone with its structure in the HslUV complex reveals several conserved amino-acid residues whose side-chain interactions differ between the two structures, suggesting that they may be part of a conformational switch that facilitates the release of the HslU carboxy-terminal helices when HslV binds.

PubMed: 11468391
DOI: 10.1107/S0907444901007673

実験手法

X-RAY DIFFRACTION (2.8 Å)