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 3.41&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1g3i.gif|left|200px]]<br /><applet load="1g3i" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1g3i" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1g3i, resolution 3.41&Aring;" />
caption="1g3i, resolution 3.41&Aring;" />
'''CRYSTAL STRUCTURE OF THE HSLUV PROTEASE-CHAPERONE COMPLEX'''<br />
'''CRYSTAL STRUCTURE OF THE HSLUV PROTEASE-CHAPERONE COMPLEX'''<br />
==Overview==
==Overview==
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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.
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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==
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1G3I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with ATP as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1G3I with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb80_1.html AAA+ Proteases]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G3I OCA].
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1G3I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. The following page contains interesting information on the relation of 1G3I with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb80_1.html AAA+ Proteases]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G3I OCA].
==Reference==
==Reference==
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[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: McKay, D.B.]]
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[[Category: McKay, D B.]]
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[[Category: Reddy, V.S.]]
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[[Category: Reddy, V S.]]
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[[Category: Sousa, M.C.]]
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[[Category: Sousa, M C.]]
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[[Category: Trame, C.B.]]
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[[Category: Trame, C B.]]
[[Category: Tsuruta, H.]]
[[Category: Tsuruta, H.]]
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[[Category: Wilbanks, S.M.]]
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[[Category: Wilbanks, S M.]]
[[Category: ATP]]
[[Category: ATP]]
[[Category: chaperone/hydrolase]]
[[Category: chaperone/hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:00:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:45:37 2008''

Revision as of 10:45, 21 February 2008


1g3i, resolution 3.41Å

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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 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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