3fbr | pdb_00003fbr

structure of HipA-amppnp-peptide

spinqualitylabelsall models 3fbr, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3fbr is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACP NonStd Res: UNK Related: 3dnt, 3dnv, 3dnw, 3dnu Gene: hipA, b1507, JW1500 (Escherichia coli) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Bacterial multidrug tolerance is largely responsible for the inability of antibiotics to eradicate infections and is caused by a small population of dormant bacteria called persisters. HipA is a critical Escherichia coli persistence factor that is normally neutralized by HipB, a transcription repressor, which also regulates hipBA expression. Here, we report multiple structures of HipA and a HipA-HipB-DNA complex. HipA has a eukaryotic serine/threonine kinase-like fold and can phosphorylate the translation factor EF-Tu, suggesting a persistence mechanism via cell stasis. The HipA-HipB-DNA structure reveals the HipB-operator binding mechanism, approximately 70 degrees DNA bending, and unexpected HipA-DNA contacts. Dimeric HipB interacts with two HipA molecules to inhibit its kinase activity through sequestration and conformational inactivation. Combined, these studies suggest mechanisms for HipA-mediated persistence and its neutralization by HipB. Molecular mechanisms of HipA-mediated multidrug tolerance and its neutralization by HipB.,Schumacher MA, Piro KM, Xu W, Hansen S, Lewis K, Brennan RG Science. 2009 Jan 16;323(5912):396-401. PMID:19150849 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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