Journal article

Characterisation of the Porphyromonas gingivalis Manganese Transport Regulator Orthologue

Lianyi Zhang, Catherine A Butler, Hasnah SG Khan, Stuart G Dashper, Christine A Seers, Paul D Veith, Jian-Guo Zhang, Eric C Reynolds

PLOS ONE | PUBLIC LIBRARY SCIENCE | Published : 2016

Abstract

PgMntR is a predicted member of the DtxR family of transcriptional repressors responsive to manganese in the anaerobic periodontal pathogen Porphyromonas gingivalis. Our bioinformatic analyses predicted that PgMntR had divalent metal binding site(s) with elements of both manganous and ferrous ion specificity and that PgMntR has unusual twin C-terminal FeoA domains. We produced recombinant PgMntR and four variants to probe the specificity of metal binding and its impact on protein structure and DNA binding. PgMntR dimerised in the absence of a divalent transition metal cation. PgMntR bound three Mn(II) per monomer with an overall dissociation constant Kd 2.0 x 10(-11) M at pH 7.5. PgMntR also..

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