title: 1H,13C and15N resonance assignments of the new lysostaphin family endopeptidase catalytic domain from Staphylococcus aureus.
abstract: Lysostaphin family endopeptidases, produced by Staphylococcus genus, are zinc-dependent enzymes that cleave pentaglycine bridges of cell wall peptidoglycan. They act as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Consequently, these enzymes are compelling targets for new drugs as well as are potential antimicrobial agents themselves against Staphylococcus pathogens, which depend on cell wall to retain their immunity against antibiotics. The rapid spread of methicillin and vancomycin-resistant Staphylococcus aureus strains draws demand for new therapeutic approaches. S. aureus gene sa0205 was found to be implicated in resistance to vancomycin and synthesis of the bacteria cell wall. The gene encodes for a catalytic domain of a lysostaphin-type endopeptidase. We aim to obtain the structure of the Sa0205 catalytic domain, the first solution structure of the catalytic domain of the lysostaphin family enzymes. In addition, we are to investigate the apparent binding of the second zinc ion, which has not been previously reported for the enzyme group. Herein, we present the backbone and side chain resonance assignments of Sa0205 endopeptidase catalytic domain in its one and two zinc-bound forms.
authors.affiliation: Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Viikinkaari 1, P.O. Box 65, 00014, Helsinki, Finland.
authors.forename: Vytas
authors.initials: V
authors.lastname: Raulinaitis
authors.affiliation: Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Viikinkaari 1, P.O. Box 65, 00014, Helsinki, Finland.
authors.forename: Helena
authors.initials: H
authors.lastname: Tossavainen
authors.affiliation: Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Viikinkaari 1, P.O. Box 65, 00014, Helsinki, Finland.|Glykos Finland Ltd., Viikinkaari 6, 00790, Helsinki, Finland.
authors.forename: Olli
authors.initials: O
authors.lastname: Aitio
authors.affiliation: Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Viikinkaari 1, P.O. Box 65, 00014, Helsinki, Finland.
authors.forename: Raili
authors.initials: R
authors.lastname: Seppala
authors.affiliation: Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, Viikinkaari 1, P.O. Box 65, 00014, Helsinki, Finland. perttu.permi@jyu.fi.|Departments of Biological and Environmental Science and Chemistry, Nanoscience Center, University of Jyvaskyla, 40014, Jyvaskyla, Finland. perttu.permi@jyu.fi.
authors.forename: Perttu
authors.identifier: 0000-0002-6281-1138
authors.initials: P
authors.lastname: Permi
mesh_terms: D000595:Amino Acid Sequence; D020134:Catalytic Domain; D008248:Lysostaphin / Q000737:chemistry* / Q000378:metabolism; D019906:Nuclear Magnetic Resonance, Biomolecular; D013211:Staphylococcus aureus / Q000201:enzymology*
chemical_list: D008248:Lysostaphin
keywords: Lysostaphin; NMR; Pentaglycine endopeptidase; Peptidoglycan; Staphylococcus aureus; Zinc