title: The endolysin-binding domain encompasses the N-terminal region of the mycobacteriophage Ms6 Gp1 chaperone.
abstract: The intermolecular interactions of the mycobacteriophage Ms6 secretion chaperone with endolysin were characterized. The 384-amino-acid lysin (lysin(384))-binding domain was found to encompass the N-terminal region of Gp1, which is also essential for a lysis phenotype in Escherichia coli. In addition, a GXXXG-like motif involved in Gp1 homo-oligomerization was identified within the C-terminal region.
authors.affiliation: Centro de Patogénese Molecular, Unidade dos Retrovírus e Infecções Associadas, Faculty of Pharmacy, University of Lisbon, Av. Prof. Gama Pinto, 1649-003 Lisbon, Portugal.
authors.forename: Maria João
authors.initials: MJ
authors.lastname: Catalão
authors.forename: Filipa
authors.initials: F
authors.lastname: Gil
authors.forename: José
authors.initials: J
authors.lastname: Moniz-Pereira
authors.forename: Madalena
authors.initials: M
authors.lastname: Pimentel
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001433:Bacteriolysis; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000502:physiology; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009160:Mycobacteriophages / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D025941:Protein Interaction Mapping; D055503:Protein Multimerization; D016415:Sequence Alignment; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D018832:Molecular Chaperones; D014764:Viral Proteins; D010450:Endopeptidases; C001143:endolysin