The three-dimensional structure of ricin at 2.8 A.

W. Montfort; J. E. Villafranca; A. F. Monzingo; S. R. Ernst; B. Katzin; E. Rutenber; N. H. Xuong; R. Hamlin; J. D. Robertus

The three-dimensional structure of ricin at 2.8 A.

W. Montfort, J. E. Villafranca, A. F. Monzingo, S. R. Ernst, B. Katzin, E. Rutenber, N. H. Xuong, R. Hamlin, J. D. Robertus

Chemistry and Biochemistry

Research output: Contribution to journal › Article › peer-review

338 Scopus citations

Abstract

The x-ray crystallographic structure of the heterodimeric plant toxin ricin has been determined at 2.8-A resolution. The A chain enzyme is a globular protein with extensive secondary structure and a reasonably prominent cleft assumed to be the active site. The B chain lectin folds into two topologically similar domains, each binding lactose in a shallow cleft. In each site a glutamine residue forms a hydrogen bond to the OH-4 of galactose, accounting for the epimerimic specificity of binding. The interface between the A and B chains shows some hydrophobic contacts in which proline and phenylalanine side chains play a prominent role.

Original language	English (US)
Pages (from-to)	5398-5403
Number of pages	6
Journal	Journal of Biological Chemistry
Volume	262
Issue number	11
State	Published - Apr 15 1987

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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title = "The three-dimensional structure of ricin at 2.8 A.",

abstract = "The x-ray crystallographic structure of the heterodimeric plant toxin ricin has been determined at 2.8-A resolution. The A chain enzyme is a globular protein with extensive secondary structure and a reasonably prominent cleft assumed to be the active site. The B chain lectin folds into two topologically similar domains, each binding lactose in a shallow cleft. In each site a glutamine residue forms a hydrogen bond to the OH-4 of galactose, accounting for the epimerimic specificity of binding. The interface between the A and B chains shows some hydrophobic contacts in which proline and phenylalanine side chains play a prominent role.",

author = "W. Montfort and Villafranca, {J. E.} and Monzingo, {A. F.} and Ernst, {S. R.} and B. Katzin and E. Rutenber and Xuong, {N. H.} and R. Hamlin and Robertus, {J. D.}",

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AU - Montfort, W.

AU - Villafranca, J. E.

AU - Monzingo, A. F.

AU - Ernst, S. R.

AU - Katzin, B.

AU - Rutenber, E.

AU - Xuong, N. H.

AU - Hamlin, R.

AU - Robertus, J. D.

PY - 1987/4/15

Y1 - 1987/4/15

N2 - The x-ray crystallographic structure of the heterodimeric plant toxin ricin has been determined at 2.8-A resolution. The A chain enzyme is a globular protein with extensive secondary structure and a reasonably prominent cleft assumed to be the active site. The B chain lectin folds into two topologically similar domains, each binding lactose in a shallow cleft. In each site a glutamine residue forms a hydrogen bond to the OH-4 of galactose, accounting for the epimerimic specificity of binding. The interface between the A and B chains shows some hydrophobic contacts in which proline and phenylalanine side chains play a prominent role.

AB - The x-ray crystallographic structure of the heterodimeric plant toxin ricin has been determined at 2.8-A resolution. The A chain enzyme is a globular protein with extensive secondary structure and a reasonably prominent cleft assumed to be the active site. The B chain lectin folds into two topologically similar domains, each binding lactose in a shallow cleft. In each site a glutamine residue forms a hydrogen bond to the OH-4 of galactose, accounting for the epimerimic specificity of binding. The interface between the A and B chains shows some hydrophobic contacts in which proline and phenylalanine side chains play a prominent role.

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