1k32: Difference between revisions

Revision as of 14:29, 21 February 2008

Crystal structure of the tricorn protease

OverviewOverview

The degradation of cytosolic proteins is carried out predominantly by the proteasome, which generates peptides of 7-9 amino acids long. These products need further processing. Recently, a proteolytic system was identified in the model organism Thermoplasma acidophilum that performs this processing. The hexameric core protein of this modular system, referred to as tricorn protease, is a 720K protease that is able to assemble further into a giant icosahedral capsid, as determined by electron microscopy. Here, we present the crystal structure of the tricorn protease at 2.0 A resolution. The structure reveals a complex mosaic protein whereby five domains combine to form one of six subunits, which further assemble to form the 3-2-symmetric core protein. The structure shows how the individual domains coordinate the specific steps of substrate processing, including channelling of the substrate to, and the product from, the catalytic site. Moreover, the structure shows how accessory protein components might contribute to an even more complex protein machinery that efficiently collects the tricorn-released products.

About this StructureAbout this Structure

1K32 is a Single protein structure of sequence from Thermoplasma acidophilum. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the tricorn protease reveals a protein disassembly line., Brandstetter H, Kim JS, Groll M, Huber R, Nature. 2001 Nov 22;414(6862):466-70. PMID:11719810

Page seeded by OCA on Thu Feb 21 13:29:31 2008

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OCA

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-[[Image:1k32.gif|left|200px]]<br /><applet load="1k32" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1k32.gif|left|200px]]<br /><applet load="1k32" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1k32, resolution 2.0&Aring;" />
 '''Crystal structure of the tricorn protease'''<br />
 ==Overview==
-The degradation of cytosolic proteins is carried out predominantly by the, proteasome, which generates peptides of 7-9 amino acids long. These, products need further processing. Recently, a proteolytic system was, identified in the model organism Thermoplasma acidophilum that performs, this processing. The hexameric core protein of this modular system, referred to as tricorn protease, is a 720K protease that is able to, assemble further into a giant icosahedral capsid, as determined by, electron microscopy. Here, we present the crystal structure of the tricorn, protease at 2.0 A resolution. The structure reveals a complex mosaic, protein whereby five domains combine to form one of six subunits, which, further assemble to form the 3-2-symmetric core protein. The structure, shows how the individual domains coordinate the specific steps of, substrate processing, including channelling of the substrate to, and the, product from, the catalytic site. Moreover, the structure shows how, accessory protein components might contribute to an even more complex, protein machinery that efficiently collects the tricorn-released products.
+The degradation of cytosolic proteins is carried out predominantly by the proteasome, which generates peptides of 7-9 amino acids long. These products need further processing. Recently, a proteolytic system was identified in the model organism Thermoplasma acidophilum that performs this processing. The hexameric core protein of this modular system, referred to as tricorn protease, is a 720K protease that is able to assemble further into a giant icosahedral capsid, as determined by electron microscopy. Here, we present the crystal structure of the tricorn protease at 2.0 A resolution. The structure reveals a complex mosaic protein whereby five domains combine to form one of six subunits, which further assemble to form the 3-2-symmetric core protein. The structure shows how the individual domains coordinate the specific steps of substrate processing, including channelling of the substrate to, and the product from, the catalytic site. Moreover, the structure shows how accessory protein components might contribute to an even more complex protein machinery that efficiently collects the tricorn-released products.
 ==About this Structure==
-K32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K32 OCA].
+K32 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K32 OCA].
 ==Reference==
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 [[Category: Groll, M.]]
 [[Category: Huber, R.]]
-[[Category: Kim, J.S.]]
+[[Category: Kim, J S.]]
 [[Category: beta propeller]]
 [[Category: proteasome]]
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 [[Category: substrate gating]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:48:42 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:31 2008''