1NYO

Solution structure of the antigenic TB protein MPT70/MPB70

Summary for 1NYO

• Entry DOI: 10.2210/pdb1nyo/pdb
• Descriptor: Immunogenic protein MPT70 (1 entity in total)
• Functional Keywords: seven-stranded beta-barrel, fasciclin domain, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, immune system
• Biological source: Mycobacterium tuberculosis
• Cellular location: Secreted: P0A668
• Total number of polymer chains: 1
• Total formula weight: 16311.12

Authors

Bloemink, M.J.,Dentten, E.,Hewinson, R.G.,Williamson, R.A.,Carr, M.D.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2003-02-13, release date: 2003-08-19, Last modification date: 2024-11-06)

Primary citation

Carr, M.D.,Bloemink, M.J.,Dentten, E.,Whelan, A.O.,Gordon, S.V.,Kelly, G.,Frenkiel, T.A.,Hewinson, R.G.,Williamson, R.A.
Solution structure of the Mycobacterium tuberculosis complex protein MPB70: from tuberculosis pathogenesis to inherited human corneal desease
J.Biol.Chem., 278:43736-43743, 2003

PubMed Abstract: The closely related mycobacteria responsible for tuberculosis produce an unusually high number of secreted proteins, many of which are clearly implicated in pathogenesis and protective immunity. Falling within this category are the closely related proteins MPB70 and MPB83. The structure of MPB70 reveals a complex and novel bacterial fold, which has clear structural homology to the two C-terminal FAS1 domains of the cell adhesion protein fasciclin I, whose structures were reported very recently. Assessment of the surface features of MPB70, the sequence divergence between MPB70 and MPB83, the conservation of residues across a group of FAS1 domains, and the locations of disease-inducing mutations in betaig-h3 strongly suggests that MPB70 and MPB83 contain two functional surfaces on opposite faces, which are probably involved in binding to host cell proteins. This analysis also suggests that these functional surfaces are retained in the FAS1 proteins associated with mediating interactions between cells and the extracellular matrix (fasciclin I, periostin, and betaig-h3) and furthermore that some of the human corneal disease-inducing substitutions identified in betaig-h3 will perturb interactions at these sites.

PubMed: 12917404
DOI: 10.1074/jbc.M307235200

Experimental method

SOLUTION NMR