1g3k
From Proteopedia
(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...) |
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| - | [[Image:1g3k.jpg|left|200px]]<br /><applet load="1g3k" size=" | + | [[Image:1g3k.jpg|left|200px]]<br /><applet load="1g3k" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g3k, resolution 1.90Å" /> | caption="1g3k, resolution 1.90Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: McKay, D B.]] |
| - | [[Category: Sousa, M | + | [[Category: Sousa, M C.]] |
[[Category: NA]] | [[Category: NA]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:40 2008'' |
Revision as of 10:45, 21 February 2008
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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 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
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