1g3i
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(New page: 200px<br /> <applet load="1g3i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g3i, resolution 3.41Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 06:53, 18 November 2007
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CRYSTAL STRUCTURE OF THE HSLUV PROTEASE-CHAPERONE COMPLEX
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
1G3I is a Protein complex structure of sequences from Haemophilus influenzae with ATP as ligand. The following page contains interesting information on the relation of 1G3I with [AAA+ Proteases]. 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
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