2k9s: Difference between revisions
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==Solution structure of dna binding domain of E. coli arac== | ==Solution structure of dna binding domain of E. coli arac== | ||
<StructureSection load='2k9s' size='340' side='right' caption='[[2k9s | <StructureSection load='2k9s' size='340' side='right'caption='[[2k9s]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k9s]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2k9s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2K9S FirstGlance]. <br> | ||
</td></tr><tr id=' | </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=2k9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9s OCA], [https://pdbe.org/2k9s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k9s RCSB], [https://www.ebi.ac.uk/pdbsum/2k9s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k9s ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ARAC_ECOLI ARAC_ECOLI] This protein controls the expression of at least six genes that are involved in the transport and catabolism of L-arabinose. It regulates initiation of transcription of the araBAD operon and it also controls its own synthesis. The L-arabinose operon displays both positive and negative regulation through AraC. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 19: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 2k9s" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2k9s" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | |||
[[Category: Rodgers ME]] | |||
[[Category: Schleif RF]] | |||
[[Category: | |||
[[Category: | |||
[[Category: | |||
Latest revision as of 12:46, 9 May 2024
Solution structure of dna binding domain of E. coli aracSolution structure of dna binding domain of E. coli arac
Structural highlights
FunctionARAC_ECOLI This protein controls the expression of at least six genes that are involved in the transport and catabolism of L-arabinose. It regulates initiation of transcription of the araBAD operon and it also controls its own synthesis. The L-arabinose operon displays both positive and negative regulation through AraC. 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. See AlsoReferences
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