Differential roles of tryptophan residues in conformational stability of Porphyromonas gingivalis HmuY hemophore.

ABSTRACT:

Background

We have previously shown that the P. gingivalis HmuY hemophore-like protein binds heme and scavenges heme from host hemoproteins to further deliver it to the cognate heme receptor HmuR. The aim of this study was to characterize structural features of HmuY variants in the presence and absence of heme with respect to roles of tryptophan residues in conformational stability.

Results

HmuY possesses tryptophan residues at positions 51 and 73, which are conserved in HmuY homologs present in a variety of bacteria, and a tryptophan residue at position 161, which has been found only in HmuY identified in P. gingivalis strains. We expressed and purified the wildtype HmuY and its protein variants with single tryptophan residues replaced by alanine or tyrosine residues. All H

SUBMITTER: Bielecki M 

PROVIDER: S-EPMC3922309 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature