1otn: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1otn.jpg|left|200px]] | [[Image:1otn.jpg|left|200px]] | ||
'''Calcium-binding mutant of the Internalin B LRR domain''' | {{Structure | ||
|PDB= 1otn |SIZE=350|CAPTION= <scene name='initialview01'>1otn</scene>, resolution 1.97Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Calcium-binding mutant of the Internalin B LRR domain''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1OTN is a [ | 1OTN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTN OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15020228 15020228] | ||
[[Category: Listeria monocytogenes]] | [[Category: Listeria monocytogenes]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 27: | Line 36: | ||
[[Category: listeria]] | [[Category: listeria]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:15:26 2008'' | ||
Revision as of 14:15, 20 March 2008
| |||||||
| , resolution 1.97Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Calcium-binding mutant of the Internalin B LRR domain
OverviewOverview
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 StructureAbout this Structure
1OTN is a Single protein structure of sequence from Listeria monocytogenes. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Thu Mar 20 13:15:26 2008