1OTO

Calcium-binding mutant of the internalin B LRR domain

Summary for 1OTO

• Entry DOI: 10.2210/pdb1oto/pdb
• Related: 1OTM 1OTN 1d0b
• Descriptor: Internalin B, CALCIUM ION (3 entities in total)
• Functional Keywords: internalin, inlb, calcium-binding, invasion, listeria, cell adhesion
• Biological source: Listeria monocytogenes
• Total number of polymer chains: 1
• Total formula weight: 26213.07

Authors

Marino, M.,Copp, J.,Dramsi, S.,Chapman, T.,van der Geer, P.,Cossart, P.,Ghosh, P. (deposition date: 2003-03-21, release date: 2004-03-30, Last modification date: 2023-08-16)

Primary citation

Marino, M.,Banerjee, M.,Copp, J.,Dramsi, S.,Chapman, T.,Van Der Geer, P.,Cossart, P.,Ghosh, P.
Characterization of the calcium-binding sites of Listeria monocytogenes InlB
Biochem.Biophys.Res.Commun., 316:379-386, 2004

PubMed Abstract: 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.

PubMed: 15020228
DOI: 10.1016/j.bbrc.2004.02.064

Experimental method

X-RAY DIFFRACTION (1.96 Å)