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New page: left|200px<br /><applet load="1g3k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g3k, resolution 1.90Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1g3k.jpg|left|200px]]<br /><applet load="1g3k" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1g3k.jpg|left|200px]]<br /><applet load="1g3k" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1g3k, resolution 1.90&Aring;" />
caption="1g3k, resolution 1.90&Aring;" />
'''CRYSTAL STRUCTURE OF THE H. INFLUENZAE PROTEASE HSLV AT 1.9 A RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF THE H. INFLUENZAE PROTEASE HSLV AT 1.9 A RESOLUTION'''<br />


==Overview==
==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.
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==
==About this Structure==
1G3K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G3K OCA].  
1G3K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G3K OCA].  


==Reference==
==Reference==
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[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: McKay, D.B.]]
[[Category: McKay, D B.]]
[[Category: Sousa, M.C.]]
[[Category: Sousa, M C.]]
[[Category: NA]]
[[Category: NA]]
[[Category: hydrolase]]
[[Category: hydrolase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:40:19 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:40 2008''