1k32: Difference between revisions

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[[Image:1k32.gif|left|200px]]
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[[Image:1k32.png|left|200px]]


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{{STRUCTURE_1k32|  PDB=1k32  |  SCENE=  }}  
{{STRUCTURE_1k32|  PDB=1k32  |  SCENE=  }}  


'''Crystal structure of the tricorn protease'''
===Crystal structure of the tricorn protease===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11719810}}


==About this Structure==
==About this Structure==
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[[Category: Serine protease]]
[[Category: Serine protease]]
[[Category: Substrate gating]]
[[Category: Substrate gating]]
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Revision as of 19:10, 1 July 2008

File:1k32.png

Template:STRUCTURE 1k32

Crystal structure of the tricorn protease

Template:ABSTRACT PUBMED 11719810

About this Structure

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

Reference

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

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