2k9s: Difference between revisions
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[[ | ==Solution structure of dna binding domain of E. coli arac== | ||
<StructureSection load='2k9s' size='340' side='right' caption='[[2k9s]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2k9s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K9S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K9S FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bl0|1bl0]], [[1d5y|1d5y]], [[2ara|2ara]], [[2arc|2arc]], [[2aac|2aac]], [[1xja|1xja]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">araC, b0064, JW0063 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=2k9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9s OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k9s RCSB], [http://www.ebi.ac.uk/pdbsum/2k9s PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We report the solution structure of the DNA binding domain of the Escherichia coli regulatory protein AraC determined in the absence of DNA. The 20 lowest energy structures, determined on the basis of 1507 unambiguous nuclear Overhauser restraints and 180 angle restraints, are well resolved with a pair wise backbone root mean square deviation of 0.7 A. The protein, free of DNA, is well folded in solution and contains seven helices arranged in two semi-independent sub domains, each containing one helix-turn-helix DNA binding motif, joined by a 19 residue central helix. This solution structure is discussed in the context of extensive biochemical and physiological data on AraC and with respect to the DNA-bound structures of the MarA and Rob homologs. Proteins 2009. (c) 2009 Wiley-Liss, Inc. | |||
Solution structure of the DNA binding domain of AraC protein.,Rodgers ME, Schleif R Proteins. 2009 Mar 24. PMID:19422057<ref>PMID:19422057</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Rodgers, M E.]] | [[Category: Rodgers, M E.]] | ||
Revision as of 18:30, 12 October 2014
Solution structure of dna binding domain of E. coli aracSolution structure of dna binding domain of E. coli arac
Structural highlights
Publication Abstract from PubMedWe report the solution structure of the DNA binding domain of the Escherichia coli regulatory protein AraC determined in the absence of DNA. The 20 lowest energy structures, determined on the basis of 1507 unambiguous nuclear Overhauser restraints and 180 angle restraints, are well resolved with a pair wise backbone root mean square deviation of 0.7 A. The protein, free of DNA, is well folded in solution and contains seven helices arranged in two semi-independent sub domains, each containing one helix-turn-helix DNA binding motif, joined by a 19 residue central helix. This solution structure is discussed in the context of extensive biochemical and physiological data on AraC and with respect to the DNA-bound structures of the MarA and Rob homologs. Proteins 2009. (c) 2009 Wiley-Liss, Inc. Solution structure of the DNA binding domain of AraC protein.,Rodgers ME, Schleif R Proteins. 2009 Mar 24. PMID:19422057[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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