1e5u: Difference between revisions
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'''NMR REPRESENTATIVE STRUCTURE OF INTIMIN-190 (INT190) FROM ENTEROPATHOGENIC E. COLI''' | '''NMR REPRESENTATIVE STRUCTURE OF INTIMIN-190 (INT190) FROM ENTEROPATHOGENIC E. COLI''' | ||
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==About this Structure== | ==About this Structure== | ||
1E5U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry | 1E5U is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1e1b 1e1b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5U OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Prasannan, S.]] | [[Category: Prasannan, S.]] | ||
[[Category: Reece, S.]] | [[Category: Reece, S.]] | ||
[[Category: | [[Category: Cell adhesion]] | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Intimin]] | ||
[[Category: | [[Category: Nmr spectroscopy]] | ||
[[Category: | [[Category: Outer membrane protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:42:06 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 14:42, 2 May 2008
NMR REPRESENTATIVE STRUCTURE OF INTIMIN-190 (INT190) FROM ENTEROPATHOGENIC E. COLI
OverviewOverview
Intimin is a bacterial adhesion molecule involved in intimate attachment of enteropathogenic and enterohaemorrhagic Escherichia coli to mammalian host cells. Intimin targets the translocated intimin receptor (Tir), which is exported by the bacteria and integrated into the host cell plasma membrane. In this study we localized the Tir-binding region of intimin to the C-terminal 190 amino acids (Int190). We have also determined the region's high-resolution solution structure, which comprises an immunoglobulin domain that is intimately coupled to a novel C-type lectin domain. This fragment, which is necessary and sufficient for Tir interaction, defines a new super domain in intimin that exhibits striking structural similarity to the integrin-binding domain of the Yersinia invasin and C-type lectin families. The extracellular portion of intimin comprises an articulated rod of immunoglobulin domains extending from the bacterium surface, conveying a highly accessible 'adhesive tip' to the target cell. The interpretation of NMR-titration and mutagenesis data has enabled us to identify, for the first time, the binding site for Tir, which is located at the extremity of the Int190 moiety.
About this StructureAbout this Structure
1E5U is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1e1b. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli., Batchelor M, Prasannan S, Daniell S, Reece S, Connerton I, Bloomberg G, Dougan G, Frankel G, Matthews S, EMBO J. 2000 Jun 1;19(11):2452-64. PMID:10835344 Page seeded by OCA on Fri May 2 14:42:06 2008