Crystal structure of abrin-a at 2.14 Å

Tahir H. Tahirov, Tian Huey Lu, Yen Chywan Liaw, Yung Liang Chen, Jung Yaw Lin

Research output: Contribution to journalArticle

139 Citations (Scopus)

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 Å to aR-factor of 18.9%. The root-mean-square deviations of bond lengths and angles from the standard values are 0.013 Å and 1.82 °, 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 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 sugar chains linked to earlier predicted glycosylation sites were determined. One of the sugar chains is a bridge between two neighbouring molecules, since one of its mannose residues is connected to the galactose binding site of the neighboring molecule. Another sugar chain covers the surface of the B-chain.

Original languageEnglish (US)
Pages (from-to)354-367
Number of pages14
JournalJournal of Molecular Biology
Volume250
Issue number3
DOIs
StatePublished - Jul 14 1995

Fingerprint

Abrin
Catalytic Domain
Ricin
Abrus
Ribosome Inactivating Proteins
Protein Folding
Lactose
Mannose
Crystallization
Galactose
Ribosomes
Glycosylation
Hydrogen
Seeds
Glycoproteins
Binding Sites
Water

Keywords

  • Abrin-a
  • Abrus precatorius
  • Antibacterial and antitumor protein
  • Ribosome-inactivating proteins
  • X-ray structure

ASJC Scopus subject areas

  • Molecular Biology

Cite this

Tahirov, T. H., Lu, T. H., Liaw, Y. C., Chen, Y. L., & Lin, J. Y. (1995). Crystal structure of abrin-a at 2.14 Å. Journal of Molecular Biology, 250(3), 354-367. https://doi.org/10.1006/jmbi.1995.0382

Crystal structure of abrin-a at 2.14 Å. / Tahirov, Tahir H.; Lu, Tian Huey; Liaw, Yen Chywan; Chen, Yung Liang; Lin, Jung Yaw.

In: Journal of Molecular Biology, Vol. 250, No. 3, 14.07.1995, p. 354-367.

Research output: Contribution to journalArticle

Tahirov, TH, Lu, TH, Liaw, YC, Chen, YL & Lin, JY 1995, 'Crystal structure of abrin-a at 2.14 Å', Journal of Molecular Biology, vol. 250, no. 3, pp. 354-367. https://doi.org/10.1006/jmbi.1995.0382
Tahirov, Tahir H. ; Lu, Tian Huey ; Liaw, Yen Chywan ; Chen, Yung Liang ; Lin, Jung Yaw. / Crystal structure of abrin-a at 2.14 Å. In: Journal of Molecular Biology. 1995 ; Vol. 250, No. 3. pp. 354-367.
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AB - 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 Å to aR-factor of 18.9%. The root-mean-square deviations of bond lengths and angles from the standard values are 0.013 Å and 1.82 °, 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 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 sugar chains linked to earlier predicted glycosylation sites were determined. One of the sugar chains is a bridge between two neighbouring molecules, since one of its mannose residues is connected to the galactose binding site of the neighboring molecule. Another sugar chain covers the surface of the B-chain.

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