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Titolo:
CRYSTAL-STRUCTURE OF ABRIN-A AT 2.14 ANGSTROM
Autore:
TAHIROV TH; LU TH; LIAW YC; CHEN YL; LIN JY;
Indirizzi:
NATL TSING HUA UNIV,DEPT PHYS HSINCHU 300 TAIWAN NATL TSING HUA UNIV,DEPT PHYS HSINCHU 300 TAIWAN ACAD SINICA,INST MOLEC BIOL TAIPEI 11529 TAIWAN NATL TAIWAN UNIV,COLL MED,INST BIOCHEM TAIPEI 10018 TAIWAN
Titolo Testata:
Journal of Molecular Biology
fascicolo: 3, volume: 250, anno: 1995,
pagine: 354 - 367
SICI:
0022-2836(1995)250:3<354:COAA2A>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
RIBOSOME-INACTIVATING PROTEINS; ABRUS-PRECATORIUS; 3-DIMENSIONAL STRUCTURE; ENZYMATIC INACTIVATION; EUKARYOTIC RIBOSOMES; GLUTAMIC ACID-177; AREA DETECTOR; B-CHAIN; RICIN; SITE;
Keywords:
ABRIN-A; RIBOSOME-INACTIVATING PROTEINS; ANTIBACTERIAL AND ANTITUMOR PROTEIN; X-RAY STRUCTURE; ABRUS PRECATORIUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
53
Recensione:
Indirizzi per estratti:
Citazione:
T.H. Tahirov et al., "CRYSTAL-STRUCTURE OF ABRIN-A AT 2.14 ANGSTROM", Journal of Molecular Biology, 250(3), 1995, pp. 354-367

Abstract

The crystal structure of abrin-a, a type II ribosome-inactivating protein from the seeds of Abrus precatorius, has been determined from a novel crystalline form by the molecular replacement method using the coordinates of ricin. The structure has been refined at 2.14 Angstrom toa R-factor of 18.9%. The root-mean-square deviations of bond lengths and angles from the standard values are 0.013 Angstrom and 1.82 degrees, respectively. The overall protein folding is similar to that of ricin, but there are differences in the secondary structure, mostly of the A-chain. Several parts of the molecular surface differ significantly; some of them are quite near the active site cleft, and probably influence ribosome recognition. The positions of invariant active site residues remain the same, except the position of Tyr74. Two water molecules of hydrogen-bonded active site residues have been located in the active site cleft. Both of them may be responsible for hydrolyzing the N-C glycosidic bond. The current abrin-a structure is lactose free; this is probably essential for abrin-a crystallization. The B-chain is a glycoprotein, and the positions of several sugar residues of two sugarchains linked to earlier predicted glycosylation sites were determined. One of the sugar chains is a bridge between two neighboring molecules, since one of its mannose residues is connected to the galactose binding site of the neighboring molecule. Another sugar chain covers thesurface of the B-chain.

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Documento generato il 05/07/20 alle ore 06:49:40