1g3i
From Proteopedia
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|PDB= 1g3i |SIZE=350|CAPTION= <scene name='initialview01'>1g3i</scene>, resolution 3.41Å | |PDB= 1g3i |SIZE=350|CAPTION= <scene name='initialview01'>1g3i</scene>, resolution 3.41Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5 | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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[[Category: chaperone/hydrolase]] | [[Category: chaperone/hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:52:36 2008'' |
Revision as of 09:52, 23 March 2008
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| , resolution 3.41Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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