Preliminary crystallographic characterization of ricin agglutinin

E. C. Sweeney; A. G. Tonevitsky; D. E. Temiakov; I. I. Agapov; S. Saward; R. A. Palmer

doi:10.1002/(SICI)1097-0134(199708)28:4<586::AID-PROT12>3.0.CO;2-C

Preliminary crystallographic characterization of ricin agglutinin

E. C. Sweeney, A. G. Tonevitsky, D. E. Temiakov, I. I. Agapov, S. Saward, R. A. Palmer

Cell Biology

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72 Scopus citations

Abstract

The quaternary structure of ricin agglutinin (RCA) has been determined by x-ray crystallography. The refined structure of ricin proved to be a successful search model using the molecular replacement method of phase determination. RCA forms an elongated molecule of dimensions 120 Å x 60 Å x 40 Å with two A chains at the center and a B chain at each end. The A chains are covalently associated via a disulfide bridge between Cys 156 of both chains. Additional contacts at residues 114-115 stabilize the dimer interface. The covalent association of RCAA chains was confirmed by gel filtration under reducing and nonreducing conditions.

Original language	English (US)
Pages (from-to)	586-589
Number of pages	4
Journal	Proteins: Structure, Function and Genetics
Volume	28
Issue number	4
DOIs	https://doi.org/10.1002/(SICI)1097-0134(199708)28:4<586::AID-PROT12>3.0.CO;2-C
State	Published - 1997

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry
Molecular Biology

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10.1002/(SICI)1097-0134(199708)28:4<586::AID-PROT12>3.0.CO;2-C

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title = "Preliminary crystallographic characterization of ricin agglutinin",

abstract = "The quaternary structure of ricin agglutinin (RCA) has been determined by x-ray crystallography. The refined structure of ricin proved to be a successful search model using the molecular replacement method of phase determination. RCA forms an elongated molecule of dimensions 120 {\AA} x 60 {\AA} x 40 {\AA} with two A chains at the center and a B chain at each end. The A chains are covalently associated via a disulfide bridge between Cys 156 of both chains. Additional contacts at residues 114-115 stabilize the dimer interface. The covalent association of RCAA chains was confirmed by gel filtration under reducing and nonreducing conditions.",

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year = "1997",

doi = "10.1002/(SICI)1097-0134(199708)28:4<586::AID-PROT12>3.0.CO;2-C",

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T1 - Preliminary crystallographic characterization of ricin agglutinin

AU - Sweeney, E. C.

AU - Tonevitsky, A. G.

AU - Temiakov, D. E.

AU - Agapov, I. I.

AU - Saward, S.

AU - Palmer, R. A.

PY - 1997

Y1 - 1997

N2 - The quaternary structure of ricin agglutinin (RCA) has been determined by x-ray crystallography. The refined structure of ricin proved to be a successful search model using the molecular replacement method of phase determination. RCA forms an elongated molecule of dimensions 120 Å x 60 Å x 40 Å with two A chains at the center and a B chain at each end. The A chains are covalently associated via a disulfide bridge between Cys 156 of both chains. Additional contacts at residues 114-115 stabilize the dimer interface. The covalent association of RCAA chains was confirmed by gel filtration under reducing and nonreducing conditions.

AB - The quaternary structure of ricin agglutinin (RCA) has been determined by x-ray crystallography. The refined structure of ricin proved to be a successful search model using the molecular replacement method of phase determination. RCA forms an elongated molecule of dimensions 120 Å x 60 Å x 40 Å with two A chains at the center and a B chain at each end. The A chains are covalently associated via a disulfide bridge between Cys 156 of both chains. Additional contacts at residues 114-115 stabilize the dimer interface. The covalent association of RCAA chains was confirmed by gel filtration under reducing and nonreducing conditions.

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JO - Proteins: Structure, Function and Genetics

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ER -

Preliminary crystallographic characterization of ricin agglutinin

Abstract

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