1q5r

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[[Image:1q5r.gif|left|200px]]
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{{Seed}}
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[[Image:1q5r.png|left|200px]]
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{{STRUCTURE_1q5r| PDB=1q5r | SCENE= }}
{{STRUCTURE_1q5r| PDB=1q5r | SCENE= }}
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'''The Rhodococcus 20S proteasome with unprocessed pro-peptides'''
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===The Rhodococcus 20S proteasome with unprocessed pro-peptides===
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==Overview==
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To understand the role of the pro-peptide in proteasome assembly, we have determined structures of the Rhodococcus proteasome and a mutant form that prevents the autocatalytic removal of its pro-peptides. The structures reveal that the pro-peptide acts as an assembly-promoting factor by linking its own beta-subunit to two adjacent alpha-subunits, thereby providing a molecular explanation for the observed kinetics of proteasome assembly. The Rhodococcus proteasome has been found to have a substantially smaller contact region between alpha-subunits compared to those regions in the proteasomes of Thermoplasma, yeast, and mammalian cells, suggesting that a smaller contact area between alpha-subunits is likely the structural basis for the Rhodococcus alpha-subunits not assembling into alpha-rings when expressed alone. Analysis of all available beta-subunit structures shows that the contact area between beta-subunits within a beta-ring is not sufficient for beta-ring self-assembly without the additional contact provided by the alpha-ring. This appears to be a fail-safe mechanism ensuring that the active sites on the beta-subunits are activated only after proteasome assembly is complete.
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The line below this paragraph, {{ABSTRACT_PUBMED_14659753}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 14659753 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14659753}}
==About this Structure==
==About this Structure==
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[[Category: Proteasome assembly]]
[[Category: Proteasome assembly]]
[[Category: Rhodococcus erythropoli]]
[[Category: Rhodococcus erythropoli]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:53:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 21:03:44 2008''

Revision as of 18:03, 27 July 2008

Template:STRUCTURE 1q5r

The Rhodococcus 20S proteasome with unprocessed pro-peptides

Template:ABSTRACT PUBMED 14659753

About this Structure

1Q5R is a Protein complex structure of sequences from Rhodococcus erythropolis. Full crystallographic information is available from OCA.

Reference

Crystal structures of the Rhodococcus proteasome with and without its pro-peptides: implications for the role of the pro-peptide in proteasome assembly., Kwon YD, Nagy I, Adams PD, Baumeister W, Jap BK, J Mol Biol. 2004 Jan 2;335(1):233-45. PMID:14659753

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