 |
PDBsum entry 5daj
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Transcription regulator
|
PDB id
|
|
|
|
5daj
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
 |
|
 |
| Name: |
 |
Transcription regulator
|
 |
|
Title:
|
 |
Crystal structure of nald, the secondary repressor of mexab-oprm multidrug efflux pump in pseudomonas aeruginosa
|
|
Structure:
|
 |
Nald. Chain: a, b, c, d, e, f, g, h. Engineered: yes
|
|
Source:
|
 |
Pseudomonas aeruginosa pao1. Organism_taxid: 208964. Gene: nald. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
|
|
Resolution:
|
 |
|
2.65Å
|
R-factor:
|
0.213
|
R-free:
|
0.266
|
|
|
Authors:
|
 |
W.Z.Chen,D.Wang,S.Q.Huang,Q.Y.Hu,X.C.Liu,J.H.Gan,H.Chen
|
|
Key ref:
|
 |
W.Chen
et al.
(2016).
Novobiocin binding to NalD induces the expression of the MexAB-OprM pump in Pseudomonas aeruginosa.
Mol Microbiol,
100,
749-758.
PubMed id:
DOI:
|
 |
|
Date:
|
 |
|
20-Aug-15
|
Release date:
|
20-Apr-16
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
Headers
|
 |
|
|
References
|
|
|
|
|
|
|
Q9HY46
(Q9HY46_PSEAE) -
NalD from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
|
|
|
|
Seq: Struc:
|
 |
 |
 |
212 a.a.
197 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
Key: |
 |
PfamA domain |
 |
 |
 |
Secondary structure |
 |
 |
CATH domain |
 |
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
DOI no:
|
Mol Microbiol
100:749-758
(2016)
|
|
PubMed id:
|
|
|
|
|
| |
|
Novobiocin binding to NalD induces the expression of the MexAB-OprM pump in Pseudomonas aeruginosa.
|
|
W.Chen,
D.Wang,
W.Zhou,
H.Sang,
X.Liu,
Z.Ge,
J.Zhang,
L.Lan,
C.G.Yang,
H.Chen.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
NalD was reported to be the secondary repressor of the MexAB-OprM multidrug
efflux pump, the major system contributing to intrinsic multidrug resistance in
Pseudomonas aeruginosa. Here, we show that novobiocin binds directly to NalD,
which leads NalD to dissociate from the DNA promoter, and thus de-represses the
expression of the MexAB-OprM pump. In addition, we have solved the crystal
structure of NalD at a resolution of 2.90 Å. The structural alignment of NalD
to its homologue TtgR reveals that the residues N129 and H167 in NalD are
involved in its novobiocin-binding ability. We have confirmed the function of
these two amino acids by EMSA and plate assay. The results presented here
highlight the importance and diversity of regulatory mechanism in bacterial
antibiotic resistance, and provide further insight for novel antimicrobial
development.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
');
}
}
 |