The endolysin-binding domain encompasses the N-terminal region of the mycobacteriophage Ms6 Gp1 chaperone.
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ABSTRACT:
SUBMITTER: Catalao MJ
PROVIDER: S-EPMC3165679 | biostudies-literature | 2011 Sep
REPOSITORIES: biostudies-literature
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The endolysin-binding domain encompasses the N-terminal region of the mycobacteriophage Ms6 Gp1 chaperone.
Catalão Maria João MJ Gil Filipa F Moniz-Pereira José J Pimentel Madalena M
Journal of bacteriology 20110715 18
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. ...[more]
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