View source for 5clv


==Crystal Structure of KorA-operator DNA complex (KorA-OA)==
<StructureSection load='5clv' size='340' side='right'caption='[[5clv]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5clv]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CLV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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=5clv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5clv OCA], [https://pdbe.org/5clv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5clv RCSB], [https://www.ebi.ac.uk/pdbsum/5clv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5clv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KORA2_ECOLX KORA2_ECOLX] In conjunction with KorB, inhibits the transcription of kilA, trfA and korAB operons. In conjunction with KorC is responsible for the negative control of kilC and kilE operons.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The IncP (Incompatibility group P) plasmids are important carriers in the spread of antibiotic resistance across Gram-negative bacteria. Gene expression in the IncP-1 plasmids is stringently controlled by a network of four global repressors, KorA, KorB, TrbA and KorC interacting cooperatively. Intriguingly, KorA and KorB can act as co-repressors at varying distances between their operators, even when they are moved to be on opposite sides of the DNA. KorA is a homodimer with the 101-amino acid subunits, folding into an N-terminal DNA-binding domain and a C-terminal dimerization domain. In this study, we have determined the structures of the free KorA repressor and two complexes each bound to a 20-bp palindromic DNA duplex containing its consensus operator sequence. Using a combination of X-ray crystallography, nuclear magnetic resonance spectroscopy, SAXS and molecular dynamics calculations, we show that the linker between the two domains is very flexible and the protein remains highly mobile in the presence of DNA. This flexibility allows the DNA-binding domains of the dimer to straddle the operator DNA on binding and is likely to be important in cooperative binding to KorB. Unexpectedly, the C-terminal domain of KorA is structurally similar to the dimerization domain of the tumour suppressor p53.

Flexibility of KorA, a plasmid-encoded, global transcription regulator, in the presence and the absence of its operator.,Rajasekar KV, Lovering AL, Dancea F, Scott DJ, Harris SA, Bingle LE, Roessle M, Thomas CM, Hyde EI, White SA Nucleic Acids Res. 2016 Mar 25. pii: gkw191. PMID:27016739<ref>PMID:27016739</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5clv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Hyde EI]]
[[Category: Rajasekar KV]]
[[Category: White SA]]