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J. Biol. Chem., Vol. 278, Issue 44, 43736-43743, October 31, 2003

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Solution Structure of the Mycobacterium tuberculosis Complex Protein MPB70

FROM TUBERCULOSIS PATHOGENESIS TO INHERITED HUMAN CORNEAL DISEASE^*

Mark D. Carr¶, Marieke J. Bloemink||, Ellen Dentten||, Adam O. Whelan**, Stephen V. Gordon**, Geoff Kelly, Thomas A. Frenkiel, R. Glyn Hewinson**, and Richard A. Williamson||

From the Department of Biochemistry, University of Leicester, Adrian Bldg., University Road, Leicester LE1 7RH, the ^||Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, the ^**TB Research Group, Department of Bacterial Diseases, Veterinary Laboratories Agency, Weybridge, New Haw, Addlestone, Surry KT15 3NB, and the Medical Research Council Biomedical NMR Centre, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom

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 ig-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 ig-h3) and furthermore that some of the human corneal disease-inducing substitutions identified in ig-h3 will perturb interactions at these sites.

Received for publication, July 7, 2003

The atomic coordinates and structure factors (code 1NYO) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by project and equipment grants from the Wellcome Trust (Grants 055394 and 047795) and by the Department for Enviroment, Food and Rural Affairs. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Both authors contributed equally to this work.

^¶ To whom correspondence should be addressed. Tel.: 44-116-252-3054; Fax: 44-116-223-1503; E-mail: mdc12{at}le.ac.uk.

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