1j2q: Difference between revisions

Revision as of 14:24, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1j2q.png

Template:STRUCTURE 1j2q

20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus

Template:ABSTRACT PUBMED 12614609

About this StructureAbout this Structure

1J2Q is a Protein complex structure of sequences from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

ReferenceReference

Investigations on the maturation and regulation of archaebacterial proteasomes., Groll M, Brandstetter H, Bartunik H, Bourenkow G, Huber R, J Mol Biol. 2003 Mar 14;327(1):75-83. PMID:12614609

Page seeded by OCA on Tue Jul 1 14:24:42 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus'''
+===20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus===
-==Overview==
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-The 20S proteasome (core particle, CP) is a multifunctional protease complex and composed of four heptameric subunit rings arranged in a hollow, barrel-shaped structure. Here, we report the crystal structure of the CP from Archaeoglobus fulgidus at 2.25A resolution. The analysis of the structure of early and late assembly intermediates of this CP gives new insights in the maturation of archaebacterial CPs and indicates similarities to assembly intermediates observed in eukaryotes. We also show a striking difference in mechanism and regulation of substrate access between eukaryotic and archaebacterial 20S proteasomes. While eukaryotic CPs are auto-inhibited by the N-terminal tails of the outer alpha-ring by imposing topological closure with a characteristic sequence motif (YDR-motif) and show regulatory gating this segment is disordered in the CP and differently structured in the alpha(7)-sub-complex of A.fulgidus leaving a pore leading into the particle with a diameter of 13A. Mutagenesis and functional studies indicate the absence of regulatory gating in the archaeal 20S proteasome.
+The line below this paragraph, {{ABSTRACT_PUBMED_12614609}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12614609}}
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 [[Category: Proteasome]]
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