This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1g3k
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1g3k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g3k, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF...)
Next diff →
Revision as of 13:33, 20 November 2007
|
CRYSTAL STRUCTURE OF THE H. INFLUENZAE PROTEASE HSLV AT 1.9 A RESOLUTION
Overview
HslUV is a "prokaryotic proteasome" composed of the HslV protease and the, HslU ATPase, a chaperone of the Clp/Hsp100 family. The 3.4 A crystal, structure of an HslUV complex is presented here. Two hexameric ATP binding, rings of HslU bind intimately to opposite sides of the HslV protease; the, HslU "intermediate domains" extend outward from the complex. The solution, structure of HslUV, derived from small angle X-ray scattering data under, conditions where the complex is assembled and active, agrees with this, crystallographic structure. When the complex forms, the carboxy-terminal, helices of HslU distend and bind between subunits of HslV, and the apical, helices of HslV shift substantially, transmitting a conformational change, to the active site region of the protease.
About this Structure
1G3K is a Single protein structure of sequence from Haemophilus influenzae with NA as ligand. Full crystallographic information is available from OCA.
Reference
Crystal and solution structures of an HslUV protease-chaperone complex., Sousa MC, Trame CB, Tsuruta H, Wilbanks SM, Reddy VS, McKay DB, Cell. 2000 Nov 10;103(4):633-43. PMID:11106733
Page seeded by OCA on Tue Nov 20 15:40:19 2007
