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| | ==NMR structure of E.coli PapI== | | ==NMR structure of E.coli PapI== |
| - | <StructureSection load='2htj' size='340' side='right'caption='[[2htj]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='2htj' size='340' side='right'caption='[[2htj]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2htj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HTJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HTJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2htj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HTJ FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2htj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2htj OCA], [http://pdbe.org/2htj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2htj RCSB], [http://www.ebi.ac.uk/pdbsum/2htj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2htj ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2htj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2htj OCA], [https://pdbe.org/2htj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2htj RCSB], [https://www.ebi.ac.uk/pdbsum/2htj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2htj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/KS71A_ECOLX KS71A_ECOLX] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dahlquist, F W]] | + | [[Category: Dahlquist FW]] |
| - | [[Category: Kawamura, T]] | + | [[Category: Kawamura T]] |
| - | [[Category: Le, L U.K]] | + | [[Category: Le LUK]] |
| - | [[Category: Zhou, H]] | + | [[Category: Zhou H]] |
| - | [[Category: Pap pili]]
| + | |
| - | [[Category: Transcription activator]]
| + | |
| - | [[Category: Winged helix-turn-helix]]
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| Structural highlights
Function
KS71A_ECOLX
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
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kawamura T, Le LU, Zhou H, Dahlquist FW. Solution structure of Escherichia coli PapI, a key regulator of the pap pili phase variation. J Mol Biol. 2007 Jan 26;365(4):1130-42. Epub 2006 Oct 25. PMID:17109885 doi:10.1016/j.jmb.2006.10.066
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