1q5r
From Proteopedia
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| - | [[Image:1q5r.gif|left|200px]] | + | [[Image:1q5r.gif|left|200px]] |
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| - | '''The Rhodococcus 20S proteasome with unprocessed pro-peptides''' | + | {{Structure |
| + | |PDB= 1q5r |SIZE=350|CAPTION= <scene name='initialview01'>1q5r</scene>, resolution 3.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] | ||
| + | |GENE= PRCA(1) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 Rhodococcus erythropolis]), PRCB(1) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 Rhodococcus erythropolis]) | ||
| + | }} | ||
| + | |||
| + | '''The Rhodococcus 20S proteasome with unprocessed pro-peptides''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Q5R is a [ | + | 1Q5R is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q5R OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14659753 14659753] |
[[Category: Proteasome endopeptidase complex]] | [[Category: Proteasome endopeptidase complex]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: Kwon, Y D.]] | [[Category: Kwon, Y D.]] | ||
[[Category: Nagy, I.]] | [[Category: Nagy, I.]] | ||
| - | [[Category: inter-subunit | + | [[Category: inter-subunit contact]] |
[[Category: pro-peptide]] | [[Category: pro-peptide]] | ||
[[Category: proteasome assembly]] | [[Category: proteasome assembly]] | ||
| - | [[Category: rhodococcus | + | [[Category: rhodococcus erythropoli]] |
| - | ''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 13:33:18 2008'' |
Revision as of 11:33, 20 March 2008
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| , resolution 3.10Å | |||||||
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| Gene: | PRCA(1) (Rhodococcus erythropolis), PRCB(1) (Rhodococcus erythropolis) | ||||||
| Activity: | Proteasome endopeptidase complex, with EC number 3.4.25.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The Rhodococcus 20S proteasome with unprocessed pro-peptides
Overview
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.
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
Page seeded by OCA on Thu Mar 20 13:33:18 2008
