1ocy: Difference between revisions

Revision as of 15:16, 21 February 2008

STRUCTURE OF THE RECEPTOR-BINDING DOMAIN OF THE BACTERIOPHAGE T4 SHORT TAIL FIBRE

OverviewOverview

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 1.5A 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.

About this StructureAbout this Structure

1OCY is a Single protein structure of sequence from Enterobacteria phage t2 with , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

The structure of the receptor-binding domain of the bacteriophage T4 short tail fibre reveals a knitted trimeric metal-binding fold., Thomassen E, Gielen G, Schutz M, Schoehn G, Abrahams JP, Miller S, van Raaij MJ, J Mol Biol. 2003 Aug 8;331(2):361-73. PMID:12888344

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OCA

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 ==Overview==
-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 1.5A 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.
+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 1.5A 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.
 ==About this Structure==
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 [[Category: Gielen, G.]]
 [[Category: Miller, S.]]
-[[Category: Raaij, M.J.Van.]]
+[[Category: Raaij, M J.Van.]]
 [[Category: Schuetz, M.]]
 [[Category: Thomassen, E.]]
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 [[Category: lipo-polysaccharide binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:56:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:15 2008''