2htj
From Proteopedia
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NMR structure of E.coli PapI
Overview
Pyelonephritis-associated pili (pap) allow uropathogenic Escherichia coli, to bind to epithelial cells and play an important role in urinary tract, infection. Expression of pap is controlled by a phase-variation mechanism, based on the two distinct heritable states that are the result of adenine, N6-methylation in either of the two GATC sequences in its regulatory, region. The methylation status of these two sequences is sensed by the, action of two proteins, Lrp and PapI, and they play a central role in, determining pap gene expression in both phase-ON and phase-OFF cells. We, used modern NMR techniques to determine the solution structure and, backbone dynamics of PapI. We found its overall fold resembles closely, that of the winged helix-turn-helix family of DNA-binding proteins. We, determined that PapI possesses its own DNA-binding activity, albeit, non-sequence-specific, independent of Lrp. PapI appears to bind to DNA, with a K(d) in the 10 microM range. Possible mechanisms by which PapI, might participate in the regulation of the pap operon are discussed in, light of these new findings.
About this Structure
2HTJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure of Escherichia coli PapI, a key regulator of the pap pili phase variation., Kawamura T, Le LU, Zhou H, Dahlquist FW, J Mol Biol. 2007 Jan 26;365(4):1130-42. Epub 2006 Oct 25. PMID:17109885
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