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PDBsum entry 5daj

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protein Protein-protein interface(s) links
Transcription regulator PDB id
5daj

 

 

 

 

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Contents
Protein chains
(+ 2 more) 197 a.a.
Waters ×10
PDB id:
5daj
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: 26844397 DOI: 10.1111/mmi.13346
Date:
20-Aug-15     Release date:   20-Apr-16    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
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: 10.1111/mmi.13346 Mol Microbiol 100:749-758 (2016)
PubMed id: 26844397  
 
 
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.
 

 

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