1LMI

1.5 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF A SECRETED PROTEIN FROM MYCOBACTERIUM TUBERCULOSIS-MPT63

Summary for 1LMI

• Entry DOI: 10.2210/pdb1lmi/pdb
• Descriptor: Immunogenic protein MPT63/MPB63 (2 entities in total)
• Functional Keywords: beta-sandwich, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, immune system
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 13749.39

Authors

Goulding, C.W.,Parseghian, A.,Sawaya, M.R.,Cascio, D.,Apostol, M.,Gennaro, M.L.,Eisenberg, D.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2002-05-01, release date: 2002-12-04, Last modification date: 2024-02-14)

Primary citation

Goulding, C.W.,Parseghian, A.,Sawaya, M.R.,Cascio, D.,Apostol, M.,Gennaro, M.L.,Eisenberg, D.
Crystal structure of a major secreted protein of Mycobacterium tuberculosis-MPT63 at 1.5-A resolution
Protein Sci., 11:2887-2893, 2002

PubMed Abstract: 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-Angstrom resolution with the hope of yielding functional information about MPT63. The structure of MPT63 is an antiparallel beta-sandwich immunoglobulin-like fold, with the unusual feature of the first beta-strand of the protein forming a parallel addition to the small antiparallel beta-sheet. MPT63 has weak structural similarity to many proteins with immunoglobulin folds, in particular, Homo sapiens beta2-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.

PubMed: 12441386
DOI: 10.1110/ps.0219002

Experimental method

X-RAY DIFFRACTION (1.5 Å)