2gop
From Proteopedia
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| - | [[Image:2gop.gif|left|200px]] | + | [[Image:2gop.gif|left|200px]] |
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| - | '''The beta-propeller domain of the Trilobed protease from Pyrococcus furiosus reveals an open velcro topology''' | + | {{Structure |
| + | |PDB= 2gop |SIZE=350|CAPTION= <scene name='initialview01'>2gop</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''The beta-propeller domain of the Trilobed protease from Pyrococcus furiosus reveals an open velcro topology''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2GOP is a [ | + | 2GOP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GOP OCA]. |
==Reference== | ==Reference== | ||
| - | The beta-propeller domain of the trilobed protease from Pyrococcus furiosus reveals an open Velcro topology., Bosch J, Tamura T, Tamura N, Baumeister W, Essen LO, Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):179-87. Epub 2007, Jan 16. PMID:[http:// | + | The beta-propeller domain of the trilobed protease from Pyrococcus furiosus reveals an open Velcro topology., Bosch J, Tamura T, Tamura N, Baumeister W, Essen LO, Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):179-87. Epub 2007, Jan 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17242511 17242511] |
[[Category: Pyrococcus furiosus]] | [[Category: Pyrococcus furiosus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: open velcro]] | [[Category: open velcro]] | ||
| - | ''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 17:07:10 2008'' |
Revision as of 15:07, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
The beta-propeller domain of the Trilobed protease from Pyrococcus furiosus reveals an open velcro topology
Overview
In the proteolytic pathway of prokaryotic and eukaryotic organisms, proteins tagged for proteolysis are firstly shredded into smaller peptides by compartmentalized proteases such as the proteasome complex. Accordingly, a variety of downstream proteases have evolved to further hydrolyze these peptides to the level of free amino acids. In the search for such downstream proteases, a high-molecular-weight protease complex called trilobed protease (TLP) was recently discovered in the archaeon Pyroccocus furiosus. The crystal structure of the N-terminal beta-propeller domain of the trilobed protease at 2 A resolution shows that the trilobed protease utilizes this accessory domain to control substrate access to the active site. Modelling of the intact TLP monomer suggests that this protease has an additional side entrance to its active site as in the DPP-IV or tricorn protease complexes.
About this Structure
2GOP is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
Reference
The beta-propeller domain of the trilobed protease from Pyrococcus furiosus reveals an open Velcro topology., Bosch J, Tamura T, Tamura N, Baumeister W, Essen LO, Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):179-87. Epub 2007, Jan 16. PMID:17242511
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