1yau

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{{STRUCTURE_1yau| PDB=1yau | SCENE= }}
{{STRUCTURE_1yau| PDB=1yau | SCENE= }}
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'''Structure of Archeabacterial 20S proteasome- PA26 complex'''
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===Structure of Archeabacterial 20S proteasome- PA26 complex===
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==Overview==
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Proteasomes are cylindrical structures that function in multiple cellular processes by degrading a wide variety of cytosolic and nuclear proteins. Substrate access and product release from the enclosed catalytic chamber occurs through axial pores that are opened by activator complexes. Here, we report high-resolution structures of wild-type and mutant archaeal proteasomes bound to the activator PA26. These structures support the proposal that an ordered open conformation is required for proteolysis and that its formation can be triggered by outward displacement of surrounding residues. The structures and associated biochemical assays reveal the mechanism of binding, which involves an interaction between the PA26 C terminus and a conserved lysine. Surprisingly, biochemical observations implicate an equivalent interaction for the unrelated ATP-dependent activators PAN and PA700.
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(as it appears on PubMed at http://www.pubmed.gov), where 15916965 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15916965}}
==About this Structure==
==About this Structure==
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[[Category: Pa26 proteasome activator 11]]
[[Category: Pa26 proteasome activator 11]]
[[Category: Proteasome 20]]
[[Category: Proteasome 20]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:05:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:44:06 2008''

Revision as of 11:44, 28 July 2008

Template:STRUCTURE 1yau

Structure of Archeabacterial 20S proteasome- PA26 complex

Template:ABSTRACT PUBMED 15916965

About this Structure

1YAU is a Protein complex structure of sequences from Thermoplasma acidophilum and Trypanosoma brucei. Full crystallographic information is available from OCA.

Reference

The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions., Forster A, Masters EI, Whitby FG, Robinson H, Hill CP, Mol Cell. 2005 May 27;18(5):589-99. PMID:15916965

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