Journal
MOLECULAR CELL
Volume 8, Issue 5, Pages 1053-1062Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(01)00396-3
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- NIGMS NIH HHS [GM29210] Funding Source: Medline
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Colicins kill E. coli by a process that involves binding to a surface receptor, entering the cell, and, finally, intoxicating it. The lethal action of colicin E3 is a specific cleavage in the ribosomal decoding A site. The crystal structure of colicin E3, reported here in a binary complex with its immunity protein (IP), reveals a Y-shaped molecule with the receptor binding domain forming a 100 Angstrom long stalk and the two globular heads of the translocation domain (T) and the catalytic domain (C) comprising the two arms. Active site residues are D510, H513, E517, and R545. IP is buried between T and C. Rather than blocking the active site, IP prevents access of the active site to the ribosome.
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