1ryp
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1ryp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ryp, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...)
Next diff →
Revision as of 23:50, 20 November 2007
|
CRYSTAL STRUCTURE OF THE 20S PROTEASOME FROM YEAST AT 2.4 ANGSTROMS RESOLUTION
Overview
The crystal structure of the 20S proteasome from the yeast Saccharomyces, cerevisiae shows that its 28 protein subunits are arranged as an, (alpha1...alpha7, beta1...beta7)2 complex in four stacked rings and occupy, unique locations. The interior of the particle, which harbours the active, sites, is only accessible by some very narrow side entrances. The, beta-type subunits are synthesized as proproteins before being, proteolytically processed for assembly into the particle. The proforms of, three of the seven different beta-type subunits, beta1/PRE3, beta2/PUP1, and beta5/PRE2, are cleaved between the threonine at position 1 and the, last glycine of the pro-sequence, with release of the active-site residue, Thr 1. These three beta-type subunits have inhibitor-binding sites, indicating that PRE2 has a chymotrypsin-like and a trypsin-like activity, and that PRE3 has peptidylglutamyl peptide hydrolytic specificity. Other, beta-type subunits are processed to an intermediate form, indicating that, an additional nonspecific endopeptidase activity may exist which is, important for peptide hydrolysis and for the generation of ligands for, class I molecules of the major histocompatibility complex.
About this Structure
1RYP is a Protein complex structure of sequences from Saccharomyces cerevisiae with MG as ligand. Active as Proteasome endopeptidase complex, with EC number 3.4.25.1 Full crystallographic information is available from OCA.
Reference
Structure of 20S proteasome from yeast at 2.4 A resolution., Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik HD, Huber R, Nature. 1997 Apr 3;386(6624):463-71. PMID:9087403
Page seeded by OCA on Wed Nov 21 01:58:03 2007
