Crystal structure of a monomeric form of severe acute respiratory syndrome coronavirus endonuclease nsp15 suggests a role for hexamerization as an allosteric switch

Mature nonstructural protein-15 (nsp15) from the severe acute respiratory syndrome coronavirus (SARS-CoV) contains a novel uridylate-specific Mn2+-dependent endoribonuclease (NendoU). Structure studies of the full-length form of the obligate hexameric enzyme from two CoVs, SARS-CoV and murine hepati...

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Bibliographic Details
Published in:	Journal of virology Vol. 81; no. 12; p. 6700
Main Authors:	Joseph, Jeremiah S, Saikatendu, Kumar Singh, Subramanian, Vanitha, Neuman, Benjamin W, Buchmeier, Michael J, Stevens, Raymond C, Kuhn, Peter
Format:	Journal Article
Language:	English
Published:	United States 01.06.2007
Subjects:	Allosteric Site Animals Binding Sites Catalytic Domain Cloning, Molecular Crystallography, X-Ray Dimerization Electrophoresis, Polyacrylamide Gel Manganese - chemistry Molecular Conformation Mutagenesis Protein Conformation RNA Replicase - chemistry SARS Virus - enzymology Viral Nonstructural Proteins - chemistry Xenopus laevis
ISSN:	0022-538X
Online Access:	Get more information
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