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.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Catalão MJ,Gil F,Moniz-Pereira J,Pimentel M

doi

10.1128/JB.00380-11

subject

Has Abstract

pub_date

2011-09-01 00:00:00

pages

5002-6

issue

18

eissn

0021-9193

issn

1098-5530

pii

JB.00380-11

journal_volume

193

pub_type

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