 |
PDBsum entry 2mp8
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Antimicrobial protein
|
PDB id
|
|
|
|
2mp8
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Identification, Characterization, And three-Dimensional structure of the novel circular bacteriocin, Enterocin nkr-5-3b, From enterococcus faecium.
|
|
|
Authors
|
|
K.Himeno,
K.J.Rosengren,
T.Inoue,
R.H.Perez,
M.L.Colgrave,
H.S.Lee,
L.Y.Chan,
S.T.Henriques,
K.Fujita,
N.Ishibashi,
T.Zendo,
P.Wilaipun,
J.Nakayama,
V.Leelawatcharamas,
H.Jikuya,
D.J.Craik,
K.Sonomoto.
|
|
|
Ref.
|
|
Biochemistry, 2015,
54,
4863-4876.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
Enterocin NKR-5-3B, one of the multiple bacteriocins produced by Enterococcus
faecium NKR-5-3, is a 64-amino acid novel circular bacteriocin that displays
broad-spectrum antimicrobial activity. Here we report the identification,
characterization, and three-dimensional nuclear magnetic resonance solution
structure determination of enterocin NKR-5-3B. Enterocin NKR-5-3B is
characterized by four helical segments that enclose a compact hydrophobic core,
which together with its circular backbone impart high stability and structural
integrity. We also report the corresponding structural gene, enkB, that encodes
an 87-amino acid precursor peptide that undergoes a yet to be described
enzymatic processing that involves adjacent cleavage and ligation of Leu(24) and
Trp(87) to yield the mature (circular) enterocin NKR-5-3B.
|
|
|
|
|
|
|
