HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Articles by Goulding, C. W. Articles by Eisenberg, D. Search for Related Content PubMed PubMed Citation Articles by Goulding, C. W. Articles by Eisenberg, D. Social Bookmarking                   What's this?

Crystal structure of a major secreted protein of Mycobacterium tuberculosis—MPT63 at 1.5-Å resolution

¹ Howard Hughes Medical Institute, University of California at Los Angeles-DOE, Center for Genomics and Proteomics, Los Angeles, California 90095, USA
² Department of Chemistry and Biochemistry, UCLA, Los Angeles, California 90095, USA
³ Public Health Research Institute, Newark, New Jersey 07103, USA

Reprint requests to: David Eisenberg, Howard Hughes Medical Institute, UCLA-DOE, Center for Genomics and Proteomics, P.O. Box 951970, Los Angeles, CA 90095, USA; e-mail: david{at}mbi.ucla.edu; fax: 310-206-3914.

MPT63 is a small, major secreted protein of unknown function from Mycobacterium tuberculosis that has been shown to have immunogenic properties and has been implicated in virulence. A BLAST search identified that MPT63 has homologs only in other mycobacteria, and is therefore mycobacteria specific. As MPT63 is a secreted protein, mycobacteria specific, and implicated in virulence, MPT63 is an attractive drug target against the deadliest infectious disease, tuberculosis (TB). As part of the TB Structural Genomics Consortium, the X-ray crystal structure of MPT63 was determined to 1.5-Ångstrom resolution with the hope of yielding functional information about MPT63. The structure of MPT63 is an antiparallel ß-sandwich immunoglobulin-like fold, with the unusual feature of the first ß-strand of the protein forming a parallel addition to the small antiparallel ß-sheet. MPT63 has weak structural similarity to many proteins with immunoglobulin folds, in particular, Homo sapiens ß2-adaptin, bovine arrestin, and Yersinia pseudotuberculosis invasin. Although the structure of MPT63 gives no conclusive evidence to its function, structural similarity suggests that MPT63 could be involved in cell-host interactions to facilitate endocytosis/phagocytosis.

Keywords: Mycobacterium tuberculosis; secreted protein MPT63; X-ray crystal structure; TB drug target; cell-host interactions

CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?