1k32
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(New page: 200px<br /><applet load="1k32" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k32, resolution 2.0Å" /> '''Crystal structure of ...)
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Revision as of 16:41, 20 November 2007
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Crystal structure of the tricorn protease
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.
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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