Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
STUDIES ON CRYSTAL-STRUCTURES, ACTIVE-CENTER GEOMETRY AND DEPURINATING MECHANISM OF 2 RIBOSOME-INACTIVATING PROTEINS
Autore:
HUANG QC; LIU SP; TANG YQ; JIN SW; WANG Y;
Indirizzi:
BEIJING UNIV,DEPT CHEM BEIJING 100871 PEOPLES R CHINA BEIJING UNIV,DEPT CHEM BEIJING 100871 PEOPLES R CHINA ACAD SINICA,SHANGHAI INST ORGAN CHEM SHANGHAI 200032 PEOPLES R CHINA
Titolo Testata:
Biochemical journal
, volume: 309, anno: 1995,
parte:, 1
pagine: 285 - 298
SICI:
0264-6021(1995)309:<285:SOCAGA>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
RICIN-A-CHAIN; N-GLYCOSIDASE ACTIVITY; AMINO-ACID-SEQUENCE; X-RAY-ANALYSIS; EUKARYOTIC RIBOSOMES; ALPHA-MOMORCHARIN; ANTIVIRAL PROTEIN; AMP NUCLEOSIDASE; TRICHOSANTHIN; SEEDS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
Q.C. Huang et al., "STUDIES ON CRYSTAL-STRUCTURES, ACTIVE-CENTER GEOMETRY AND DEPURINATING MECHANISM OF 2 RIBOSOME-INACTIVATING PROTEINS", Biochemical journal, 309, 1995, pp. 285-298

Abstract

Two ribosome-inactivating proteins, trichosanthin and alpha-momorcharin, have been studied in the forms of complexes with ATP or formycin, by an X-ray-crystallographic method at 1.6-2.0 Angstrom (0.16-0.20 nm)resolution. The native alpha-momorcharin had been studied at 2.2 Angstrom resolution, Structures of trichosanthin were determined by a multiple isomorphous replacement method. Structures of alpha-mormocharin were determined by a molecular replacement method using refined trichosanthin as the searching model. Small ligands in all these complexes have been recognized and built on the difference in electron density. All these structures have been refined to achieve good results, both in terms of crystallography and of ideal geometry. These two proteins show considerable similarity in their three-dimensional folding and to that of related proteins. On the basis of these structures, detailed geometries of the active centres of these two proteins are described and are compared with those of related proteins. In all complexes the interactions between ligand atoms and protein atoms, including hydrophobicforces, aromatic stacking interactions and hydrogen bonds, are found to be specific towards the adenine base. The relationship between the sequence conservation of ribosome-inactivating proteins and their active-centre geometry was analysed. A depurinating mechanism of ribosome-inactivating proteins is proposed on the basis of these results. The N-7 atom of the substrate base group is proposed to be protonated by anacidic residue in the active centre.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/09/20 alle ore 11:07:39