title: (1)H, (15)N, and (13)C resonance assignments of Staphylococcus aureus extracellular adherence protein domain 4.
abstract: The pathogenic bacterium Staphylococcus aureus has evolved to actively evade many aspects of the human innate immune system by expressing a series of secreted inhibitory proteins. Among these, the extracellular adherence protein (Eap) has been shown to inhibit the classical and lectin pathways of the complement system. By binding to complement component C4b, Eap is able to inhibit formation of the CP/LP C3 pro-convertase. Secreted full-length, mature Eap consists of four ~98 residue domains, all of which adopt a similar beta-grasp fold, and are connected through a short linker region. Through multiple biochemical approaches, it has been determined that the third and fourth domains of Eap are responsible for C4b binding. Here we report the backbone and side-chain resonance assignments of the 11.3 kDa fourth domain of Eap. The assignment data has been deposited in the BMRB database under the accession number 26726.
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Kansas State University, 141 Chalmers Hall, Manhattan, KS, 66506, USA.
authors.forename: Jordan L
authors.initials: JL
authors.lastname: Woehl
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Kansas State University, 141 Chalmers Hall, Manhattan, KS, 66506, USA.
authors.forename: Daisuke
authors.initials: D
authors.lastname: Takahashi
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Kansas State University, 141 Chalmers Hall, Manhattan, KS, 66506, USA.
authors.forename: Alvaro I
authors.initials: AI
authors.lastname: Herrera
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Kansas State University, 141 Chalmers Hall, Manhattan, KS, 66506, USA.
authors.forename: Brian V
authors.initials: BV
authors.lastname: Geisbrecht
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Kansas State University, 141 Chalmers Hall, Manhattan, KS, 66506, USA. omp@ksu.edu.
authors.forename: Om
authors.identifier: 0000-0001-7714-641X
authors.initials: O
authors.lastname: Prakash
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D000072417:Protein Domains; D016601:RNA-Binding Proteins / Q000737:chemistry*; D013211:Staphylococcus aureus
chemical_list: D001426:Bacterial Proteins; C444739:Eap-N protein, Staphylococcus aureus; D016601:RNA-Binding Proteins
keywords: Extracellular adherence protein; NMR; Resonance assignment; Staphylococcus aureus; Virulence factor