Structural significance of the β1K396 residue found in the Porphyromonas gingivalis sialidase β-propeller domain: a computational study with implications for novel therapeutics against periodontal disease.

ABSTRACT: Porphyromonas gingivalis sialidase activity is associated with virulence and initiated by sialic acid (SA) binding to the β-propeller domain (BPD). Sialidase BPD is structurally conserved in various bacterial species and the protein binding interfaces have the tendency to form salt bridges, whereas uncommitted charged residues may affect binding and protein structure. However, it is not clear whether the sialidase BPD of varying strains of the same bacterial species differ, particularly with regards to salt bridge formation. Here, we determined the P. gingivalis ATCC 33277 and W50 sialidase homology models and sialidase activities, while the putative salt bridge residues found in the sialidase BPDs were compared. We established that both ATCC 33277 and W50 have different sialidase homology

SUBMITTER: Cueno ME 

PROVIDER: S-EPMC4150393 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature