1g41
From Proteopedia
|
CRYSTAL STRUCTURE OF HSLU HAEMOPHILUS INFLUENZAE
Overview
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.
About this Structure
1G41 is a Single protein structure of sequence from Haemophilus influenzae with SO4 and ADP as ligands. Full crystallographic information is available from OCA.
Reference
Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning., Trame CB, McKay DB, Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1079-90. Epub 2001, Jul 23. PMID:11468391
Page seeded by OCA on Tue Nov 20 15:41:09 2007
