1k32
From Proteopedia
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| - | [[Image:1k32.gif|left|200px]] | + | [[Image:1k32.gif|left|200px]] |
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| - | '''Crystal structure of the tricorn protease''' | + | {{Structure |
| + | |PDB= 1k32 |SIZE=350|CAPTION= <scene name='initialview01'>1k32</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= TA1490 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of the tricorn protease''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1K32 is a [ | + | 1K32 is a [[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== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11719810 11719810] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermoplasma acidophilum]] | [[Category: Thermoplasma acidophilum]] | ||
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[[Category: substrate gating]] | [[Category: substrate gating]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:11:55 2008'' |
Revision as of 10:12, 20 March 2008
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| , resolution 2.0Å | |||||||
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| Gene: | TA1490 (Thermoplasma acidophilum) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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