1oto

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(New page: 200px<br /><applet load="1oto" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oto, resolution 1.96&Aring;" /> '''Calcium-binding muta...)
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[[Image:1oto.jpg|left|200px]]<br /><applet load="1oto" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1oto.jpg|left|200px]]<br /><applet load="1oto" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1oto, resolution 1.96&Aring;" />
caption="1oto, resolution 1.96&Aring;" />
'''Calcium-binding mutant of the internalin B LRR domain'''<br />
'''Calcium-binding mutant of the internalin B LRR domain'''<br />
==Overview==
==Overview==
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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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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.
==About this Structure==
==About this Structure==
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1OTO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OTO OCA].
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1OTO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTO OCA].
==Reference==
==Reference==
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[[Category: Cossart, P.]]
[[Category: Cossart, P.]]
[[Category: Dramsi, S.]]
[[Category: Dramsi, S.]]
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[[Category: Geer, P.van.der.]]
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[[Category: Geer, P van der.]]
[[Category: Ghosh, P.]]
[[Category: Ghosh, P.]]
[[Category: Marino, M.]]
[[Category: Marino, M.]]
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[[Category: listeria]]
[[Category: listeria]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:11:38 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:31 2008''

Revision as of 12:21, 21 February 2008

Image:1oto.jpg

1oto, resolution 1.96Å

Drag the structure with the mouse to rotate

Calcium-binding mutant of the internalin B LRR domain

Overview

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.

About this Structure

1OTO is a Single protein structure of sequence from Listeria monocytogenes with as ligand. Full crystallographic information is available from OCA.

Reference

Characterization of the calcium-binding sites of Listeria monocytogenes InlB., Marino M, Banerjee M, Copp J, Dramsi S, Chapman T, van der Geer P, Cossart P, Ghosh P, Biochem Biophys Res Commun. 2004 Apr 2;316(2):379-86. PMID:15020228

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