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5H9T

Crystal structure of native NalD at resolution of 2.9, the secondary repressor of MexAB-OprM multidrug efflux pump in Pseudomonas aeruginosa

Summary for 5H9T
Entry DOI10.2210/pdb5h9t/pdb
Related5DAJ
DescriptorNalD (2 entities in total)
Functional Keywordsrepressor, tetr family, transcription regulator
Biological sourcePseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Total number of polymer chains8
Total formula weight196432.97
Authors
Chen, W.Z.,Wang, D.,Huang, S.Q.,Hu, Q.Y.,Liu, X.C.,Gan, J.H.,Chen, H. (deposition date: 2015-12-29, release date: 2016-04-20, Last modification date: 2023-11-08)
Primary citationChen, W.,Wang, D.,Zhou, W.,Sang, H.,Liu, X.,Ge, Z.,Zhang, J.,Lan, L.,Yang, C.G.,Chen, H.
Novobiocin binding to NalD induces the expression of the MexAB-OprM pump in Pseudomonas aeruginosa.
Mol. Microbiol., 100:749-758, 2016
Cited by
PubMed 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.
PubMed: 26844397
DOI: 10.1111/mmi.13346
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.89 Å)
Structure validation

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