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PDBsum entry 1oto
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Cell adhesion
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PDB id
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1oto
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Characterization of the calcium-Binding sites of listeria monocytogenes inlb.
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Authors
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M.Marino,
M.Banerjee,
J.Copp,
S.Dramsi,
T.Chapman,
P.Van der geer,
P.Cossart,
P.Ghosh.
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Ref.
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Biochem Biophys Res Commun, 2004,
316,
379-386.
[DOI no: ]
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PubMed id
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Abstract
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The Listeria monocytogenes protein InlB promotes invasion of mammalian cells
through activation of the receptor tyrosine kinase Met. The InlB N-cap, a
approximately 40 residue part of the domain that binds Met, was previously
observed to bind two calcium ions in a novel and unusually exposed manner.
Because subsequent work raised questions about the existence of these
calcium-binding sites, we assayed calcium binding in solution to the InlB N-cap.
We show that calcium ions are bound with dissociation constants in the low
micromolar range at the two identified sites, and that the sites interact with
one another. We demonstrate that the calcium ions are not required for
structure, and also find that they have no appreciable effect on Met activation
or intracellular invasion. Therefore, our results indicate that the sites are
fortuitous in InlB, but also suggest that the simple architecture of the sites
may be adaptable for protein engineering purposes.
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