title: NMR Structure and Dynamics of the Resuscitation Promoting Factor RpfC Catalytic Domain.
abstract: Mycobacterium tuberculosis latent infection is maintained for years with no clinical symptoms and no adverse effects for the host. The mechanism through which dormant M. tuberculosis resuscitates and enters the cell cycle leading to tuberculosis is attracting much interest. The RPF family of proteins has been found to be responsible for bacteria resuscitation and normal proliferation. This family of proteins in M. tuberculosis is composed by five homologues (named RpfA-E) and understanding their conformational, structural and functional peculiarities is crucial to the design of therapeutic strategies.Therefore, we report the structural and dynamics characterization of the catalytic domain of RpfC from M. tubercolosis by combining Nuclear Magnetic Resonance, Circular Dichroism and Molecular Dynamics data. We also show how the formation of a disulfide bridge, highly conserved among the homologues, is likely to modulate the shape of the RpfC hydrophobic catalytic cleft. This might result in a protein function regulation via a "conformational editing" through a disulfide bond formation.
authors.affiliation: Dipartimento di Scienze e Tecnologie Ambientali Biologiche e Farmaceutiche, Second University of Naples, via Vivaldi 43, 81100, Caserta, Italy.
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Maione
authors.affiliation: Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy.
authors.forename: Alessia
authors.initials: A
authors.lastname: Ruggiero
authors.affiliation: Centro Interuniversitario di Ricerca sui Peptidi Bioattivi-University of Naples "Federico II", Via Mezzocannone 16, 80134, Napoli, Italy.
authors.forename: Luigi
authors.initials: L
authors.lastname: Russo
authors.affiliation: Faculty of Natural Sciences, Department of Life Sciences, Imperial College, 603 Sir Ernst Chain Building-South Kensington Campus, London, United Kingdom.
authors.forename: Alfonso
authors.initials: A
authors.lastname: De Simone
authors.affiliation: Dipartimento di Scienze e Tecnologie Ambientali Biologiche e Farmaceutiche, Second University of Naples, via Vivaldi 43, 81100, Caserta, Italy.|Centro Interuniversitario di Ricerca sui Peptidi Bioattivi-University of Naples "Federico II", Via Mezzocannone 16, 80134, Napoli, Italy.
authors.forename: Paolo Vincenzo
authors.initials: PV
authors.lastname: Pedone
authors.affiliation: Dipartimento di Scienze e Tecnologie Ambientali Biologiche e Farmaceutiche, Second University of Naples, via Vivaldi 43, 81100, Caserta, Italy.
authors.forename: Gaetano
authors.initials: G
authors.lastname: Malgieri
authors.affiliation: Istituto di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 16, 80134, Napoli, Italy.
authors.forename: Rita
authors.initials: R
authors.lastname: Berisio
authors.affiliation: Dipartimento di Scienze e Tecnologie Ambientali Biologiche e Farmaceutiche, Second University of Naples, via Vivaldi 43, 81100, Caserta, Italy.|Centro Interuniversitario di Ricerca sui Peptidi Bioattivi-University of Naples "Federico II", Via Mezzocannone 16, 80134, Napoli, Italy.
authors.forename: Carla
authors.initials: C
authors.lastname: Isernia
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020134:Catalytic Domain; D002942:Circular Dichroism; D003001:Cloning, Molecular; D009682:Magnetic Resonance Spectroscopy; D056004:Molecular Dynamics Simulation; D009169:Mycobacterium tuberculosis / Q000378:metabolism*; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D011994:Recombinant Proteins