1D0B
INTERNALIN B LEUCINE RICH REPEAT DOMAIN
Summary for 1D0B
Entry DOI | 10.2210/pdb1d0b/pdb |
Descriptor | INTERNALIN B, CALCIUM ION (3 entities in total) |
Functional Keywords | leucine rich repeat, calcium binding, cell adhesion |
Biological source | Listeria monocytogenes |
Total number of polymer chains | 1 |
Total formula weight | 23836.43 |
Authors | Marino, M.,Braun, L.,Cossart, P.,Ghosh, P. (deposition date: 1999-09-09, release date: 2000-01-07, Last modification date: 2024-02-07) |
Primary citation | Marino, M.,Braun, L.,Cossart, P.,Ghosh, P. Structure of the lnlB leucine-rich repeats, a domain that triggers host cell invasion by the bacterial pathogen L. monocytogenes. Mol.Cell, 4:1063-1072, 1999 Cited by PubMed Abstract: The L. monocytogenes protein lnlB activates phosphoinositide 3-kinase and induces phagocytosis in several mammalian cell types. The 1.86 A resolution X-ray crystal structure of the leucine-rich repeat domain of lnlB that is both necessary and sufficient to induce phagocytosis is presented here. The structure supports a crucial role for calcium in host cell invasion by L. monocytogenes and supplies a rationale for its function. Calciums are bound to the protein in an unusually exposed manner that suggests that the metals may act as a bridge between lnlB and mammalian cell surface receptors. The structure also identifies surfaces on the curved and elongated molecule that may constitute additional interaction sites in forming a bacterial-mammalian signaling complex. PubMed: 10635330DOI: 10.1016/S1097-2765(00)80234-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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