2mw2 | pdb_00002mw2

Hha-H-NS46 charge zipper complex

spinqualitylabelsall models 2mw2 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mw2 is a 3 chain structure with sequence from Escherichia coli K-12. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HHA_ECOLI Down-regulates hemolysin production and can also stimulate transposition events in vivo. Binds DNA and influences DNA topology in response to environmental stimuli. Involved in persister cell formation, acting downstream of mRNA interferase (toxin) MqsR. Decreases biofilm formation by repressing the transcription of fimbrial genes fimA and ihfA, and by repressing the transcription of tRNAs corresponding to rare codons, which are abundant in type 1 fimbrial genes. Publication Abstract from PubMed The Hha/YmoA nucleoid-associated proteins help selectively silence horizontally acquired genetic material, including pathogenicity and antibiotic resistance genes and their maintenance in the absence of selective pressure. Members of the Hha family contribute to gene silencing by binding to the N-terminal dimerization domain of H-NS and modifying its selectivity. Hha-like proteins and the H-NS N-terminal domain are unusually rich in charged residues, and their interaction is mostly electrostatic-driven but, nonetheless, highly selective. The NMR-based structural model of the complex between Hha/YmoA and the H-NS N-terminal dimerization domain reveals that the origin of the selectivity is the formation of a three-protein charge zipper with interdigitated complementary charged residues from Hha and the two units of the H-NS dimer. The free form of YmoA shows collective microsecond-millisecond dynamics that can by measured by NMR relaxation dispersion experiments and shows a linear dependence with the salt concentration. The number of residues sensing the collective dynamics and the population of the minor form increased in the presence of H-NS. Additionally, a single residue mutation in YmoA (D43N) abolished H-NS binding and the dynamics of the apo-form, suggesting the dynamics and binding are functionally related. A Three-protein Charge Zipper Stabilizes a Complex Modulating Bacterial Gene Silencing.,Cordeiro TN, Garcia J, Bernado P, Millet O, Pons M J Biol Chem. 2015 Aug 28;290(35):21200-12. doi: 10.1074/jbc.M114.630400. Epub, 2015 Jun 17. PMID:26085102 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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