1q5r
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|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]) | |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]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1q5q|1Q5Q]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q5r OCA], [http://www.ebi.ac.uk/pdbsum/1q5r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q5r RCSB]</span> | ||
}} | }} | ||
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[[Category: rhodococcus erythropoli]] | [[Category: rhodococcus erythropoli]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:09:09 2008'' |
Revision as of 20:09, 30 March 2008
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| , resolution 3.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | PRCA(1) (Rhodococcus erythropolis), PRCB(1) (Rhodococcus erythropolis) | ||||||
| Activity: | Proteasome endopeptidase complex, with EC number 3.4.25.1 | ||||||
| Related: | 1Q5Q
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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