1k32: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE= TA1490 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum])
|GENE= TA1490 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum])
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k32 OCA], [http://www.ebi.ac.uk/pdbsum/1k32 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k32 RCSB]</span>
}}
}}


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[[Category: substrate gating]]
[[Category: substrate gating]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:11:55 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:42:41 2008''

Revision as of 21:42, 30 March 2008

File:1k32.gif


PDB ID 1k32

Drag the structure with the mouse to rotate
, resolution 2.0Å
Gene: TA1490 (Thermoplasma acidophilum)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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