1nyo

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spinqualitylabelsall models PDB ID 1nyo Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
Gene:	mpt70/mpb70 (Mycobacterium tuberculosis)
Domains:	Fasciclin
Resources:	FirstGlance, OCA, PDBsum, JenaLib, RCSB
Coordinates:	save as pdb, mmCIF, xml

Solution structure of the antigenic TB protein MPT70/MPB70

Overview

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.

About this Structure

1NYO is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Solution structure of the Mycobacterium tuberculosis complex protein MPB70: from tuberculosis pathogenesis to inherited human corneal desease., Carr MD, Bloemink MJ, Dentten E, Whelan AO, Gordon SV, Kelly G, Frenkiel TA, Hewinson RG, Williamson RA, J Biol Chem. 2003 Oct 31;278(44):43736-43. Epub 2003 Aug 12. PMID:12917404

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