Preliminary crystallographic characterization of ricin agglutinin

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 × 60 Å × 40 Å with...

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Bibliographic Details
Published in:Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1997-08, Vol.28 (4), p.586-589
Main Authors: Sweeney, E. C., Tonevitsky, A. G., Temiakov, D. E., Agapov, I. I., Saward, S., Palmer, R. A.
Format: Article
Language:English
Subjects:
Crystallography, X-Ray
dimer formation
Lectins - chemistry
Models, Molecular
molecular replacement
Plant Lectins
Protein Conformation
ribosome inactivating protein
ricin
RIP
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Summary: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 × 60 Å × 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 RCA A chains was confirmed by gel filtration under reducing and nonreducing conditions. Proteins 28:586–589, 1997. © 1997 Wiley‐Liss, Inc.
ISSN:0887-3585
1097-0134
DOI:10.1002/(SICI)1097-0134(199708)28:4<586::AID-PROT12>3.0.CO;2-C