1RYP

CRYSTAL STRUCTURE OF THE 20S PROTEASOME FROM YEAST AT 2.4 ANGSTROMS RESOLUTION

1RYP の概要

• エントリーDOI: 10.2210/pdb1ryp/pdb
• 分子名称: 20S PROTEASOME, MAGNESIUM ION, ... (16 entities in total)
• 機能のキーワード: multicatalytic proteinase, 20s proteasome, protein degradation, antigen processing, hydrolase, protease
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Cytoplasm: P21243 P25451 P22141 P30656 P23724 P30657 P23639 P23638 P40303 P32379 P40302 P21242 P38624 P25043
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 706516.53

構造登録者

Groll, M.,Ditzel, L.,Loewe, J.,Stock, D.,Bochtler, M.,Bartunik, H.D.,Huber, R. (登録日: 1997-02-26, 公開日: 1998-04-15, 最終更新日: 2024-05-22)

主引用文献

Groll, M.,Ditzel, L.,Lowe, J.,Stock, D.,Bochtler, M.,Bartunik, H.D.,Huber, R.
Structure of 20S proteasome from yeast at 2.4 A resolution.
Nature, 386:463-471, 1997

PubMed Abstract: 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.

PubMed: 9087403
DOI: 10.1038/386463a0

実験手法

X-RAY DIFFRACTION (1.9 Å)