Cell surface proteins in archaeal and bacterial genomes comprising "LVIVD", "RIVW" and "LGxL" tandem sequence repeats are predicted to fold as beta-propeller.

Proteins that share even low sequence homologies are known to adopt similar folds. The beta-propeller structural motif is one such example. Identifying sequences that adopt a beta-propeller fold is useful to annotate protein structure and function.

Analysis and modeling of mycolyl-transferases in the CMN group.

Mycolyl-transferases are a family of proteins that are specifically present in the CMN (Corynebacterium, Mycobacterium and Nocardia) genera and are responsible for the synthesis of cell wall components. We modeled the three-dimensional structures of mycolyl-transfersases from Corynebacterium and Nocardia using homology modeling methods based on the crystal structures of mycolyl-transferases from M. tuberculosis.

The Rv3799-Rv3807 gene cluster in Mycobacterium tuberculosis genome corresponds to the 'Ancient Conserved Region' in CMN mycolyltransferases.

We have identified based on gene cluster analysis that the genes between Rv3799-Rv3807 in M. tuberculosis have orthologs in Corynebacteria, Mycobacteria and Nocardia (CMN) genomes. Therefore, this gene cluster possibly corresponds to the 'Ancient Conserved Region' of CMN mycolyltransferases.

Three-dimensional models and structure analysis of corynemycolyltransferases in Corynebacterium glutamicum and Corynebacterium efficiens.

The corynemycolyltransferase proteins were identified from Corynebacterium glutamicum and Corynebacterium efficiens genomes using computational tools available in the public domain. Three-dimensional models were constructed for corynemycolyltransferases based on the crystal structures of related mycolyltransferases in Mycobacterium tuberculosis using the comparative modeling methods. The corynemycolyltransferases share overall an alpha/beta-fold characteristic of the mycolyltransferases despite low sequence identity (<20%) shared by some of the corynemycolyltransferases.

Sequence analysis corresponding to the PPE and PE proteins in Mycobacterium tuberculosis and other genomes.

Amino acid sequence analysis corresponding to the PPE proteins in H37Rv and CDC1551 strains of the Mycobacterium tuberculosis genomes resulted in the identification of a previously uncharacterized 225 amino acid-residue common region in 22 proteins. The pairwise sequence identities were as low as 18%. Conservation of amino acid residues was observed at fifteen positions that were distributed over the whole length of the region.