PDBsum entry 1otm

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protein links
Cell adhesion PDB id
Protein chain
207 a.a. *
Waters ×123
* Residue conservation analysis
PDB id:
Name: Cell adhesion
Title: Calcium-binding mutant of the internalin b lrr domain
Structure: Internalin b. Chain: a. Fragment: lrr domain. Engineered: yes. Mutation: yes
Source: Listeria monocytogenes. Organism_taxid: 1639. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
1.93Å     R-factor:   0.201     R-free:   0.240
Authors: M.Marino,J.Copp,S.Dramsi,T.Chapman,P.Van Der Geer,P.Cossart, P.Ghosh
Key ref: M.Marino et al. (2004). Characterization of the calcium-binding sites of Listeria monocytogenes InlB. Biochem Biophys Res Commun, 316, 379-386. PubMed id: 15020228 DOI: 10.1016/j.bbrc.2004.02.064
21-Mar-03     Release date:   30-Mar-04    
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Protein chain
Pfam   ArchSchema ?
P25147  (INLB_LISMO) -  Internalin B
630 a.a.
207 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)


DOI no: 10.1016/j.bbrc.2004.02.064 Biochem Biophys Res Commun 316:379-386 (2004)
PubMed id: 15020228  
Characterization of the calcium-binding sites of Listeria monocytogenes InlB.
M.Marino, M.Banerjee, J.Copp, S.Dramsi, T.Chapman, P.van der Geer, P.Cossart, P.Ghosh.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
17517123 N.Matsushima, T.Tanaka, P.Enkhbayar, T.Mikami, M.Taga, K.Yamada, and Y.Kuroki (2007).
Comparative sequence analysis of leucine-rich repeats (LRRs) within vertebrate toll-like receptors.
  BMC Genomics, 8, 124.  
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