2JXR

STRUCTURE OF YEAST PROTEINASE A

「1JXR」から置き換えられました

2JXR の概要

• エントリーDOI: 10.2210/pdb2jxr/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000416
• 分子名称: PROTEINASE A, alpha-D-mannopyranose-(1-2)-beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, N-(morpholin-4-ylcarbonyl)-L-phenylalanyl-N-[(1R)-1-(cyclohexylmethyl)-3,3-difluoro-2,2-dihydroxy-4-(methylamino)-4-oxobutyl]-L-norleucinamide, ... (5 entities in total)
• 機能のキーワード: hydrolase-hydrolase inhibitor complex, aspartyl protease, glycoprotein, zymogen, hydrolase/hydrolase inhibitor
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37560.34

構造登録者

Aguilar, C.F.,Badasso, M.,Dreyer, T.,Cronin, N.B.,Newman, M.P.,Cooper, J.B.,Hoover, D.J.,Wood, S.P.,Johnson, M.S.,Blundell, T.L. (登録日: 1997-04-24, 公開日: 1997-10-29, 最終更新日: 2024-10-30)

主引用文献

Aguilar, C.F.,Cronin, N.B.,Badasso, M.,Dreyer, T.,Newman, M.P.,Cooper, J.B.,Hoover, D.J.,Wood, S.P.,Johnson, M.S.,Blundell, T.L.
The three-dimensional structure at 2.4 A resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae.
J.Mol.Biol., 267:899-915, 1997

PubMed Abstract: The crystal structures of glycosylated native proteinase A, an aspartic proteinase found in the vacuole of Saccharomyces cerevisiae, and its complex with a difluorostatone-containing tripeptide have been determined by molecular replacement to 3.5 A and 2.4 A resolutions, respectively. Superposition of the bound and native forms gave an r.m.s. difference of 0.6 A largely reflecting the poor resolution of the native crystal structure. The secondary and tertiary structures are highly similar to those found in porcine pepsin and lysosomal cathepsin D; superposition of the structure of proteinase A bound to the difluorostatone inhibitor on those of pepsin and cathepsin D gave pairwise r.m.s. differences for C(alpha) atoms of 1.36 A and 0.88 A. Most differences occur in loop regions. Comparison of the structure of the proteinase A-difluorostatone complex with that of endothiapepsin bound with the same inhibitor shows that the conformation and hydrogen bond interactions of the inhibitor in the active site are very similar, even though the enzymes have only 27% sequence identity. Electron density for the crystal structure of the proteinase A complex reveals five residues of the oligosaccharide structure attached to Asn67: Man-(1 --> 2)-alpha-Man-(1 --> 3)-beta-Man-(1 --> 4)-beta-GlcNAc-(1 --> 4)-beta-GlcNAc-Asn-67. The first three residues of the oligosaccharide cover the same region of the protein surface as those of the oligosaccharide attached to the equivalent position in cathepsin D. The second carbohydrate attachment site is disordered beyond the first carbohydrate residue in both enzymes.

PubMed: 9135120
DOI: 10.1006/jmbi.1996.0880

実験手法

X-RAY DIFFRACTION (2.4 Å)