Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 331, Issue 2, Pages 361-373Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/s0022-2836(03)00755-1
Keywords
gene product 12; short fibre; receptor-binding; intertwined strands; domain swapping
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Adsorption of T4 bacteriophage to the Escherichia coli host cell is mediated by six long and six short tail fibres. After at least three long tail fibres have bound, short tail fibres extend and bind irreversibly to the core region of the host cell lipo-polysaccharide (LPS), serving as inextensible stays during penetration of the cell envelope by the tail tube. The short tail fibres consist of a parallel, in-register, trimer of gene product 12 (gP12). X-ray crystallography at 1.5 Angstrom resolution of a protease-stable fragment of gp12 generated in the presence of zinc chloride reveals the structure of the C-terminal receptor-binding domain. It has a novel knitted fold, consisting of three extensively intertwined monomers. It reveals a metal-binding site, containing a zinc ion coordinated by six histidine residues in an octahedral conformation. We also suggest an LPS-binding region. (C) 2003 Elsevier Ltd. All rights reserved.
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