2lw1: Difference between revisions
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==The C-terminal domain of the Uup protein is a DNA-binding coiled coil motif== | |||
<StructureSection load='2lw1' size='340' side='right'caption='[[2lw1]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2lw1]] 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=2LW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LW1 FirstGlance]. <br> | |||
</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=2lw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lw1 OCA], [https://pdbe.org/2lw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lw1 RCSB], [https://www.ebi.ac.uk/pdbsum/2lw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lw1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/UUP_ECOLI UUP_ECOLI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The bacterial Uup protein belongs to the REG subfamily of soluble ATP-binding cassette (ABC) ATPases, and is implicated in precise excision of transposons. In Escherichia coli, the uup gene encodes a 72kDa polypeptide that comprises two ABC domains, separated by a linker region, and a 12kDa C-terminal domain (CTD). Uup binds double-stranded DNA with no sequence specificity, and we previously demonstrated that the CTD domain is a crucial region that participates in DNA-binding activity. We report herein the NMR structure of Uup CTD, consisting of an intramolecular antiparallel two-stranded coiled coil motif. Structural comparison with analogous coiled coil domains reveals that Uup CTD contains an atypical 3(10)-helix in the alpha-hairpin region that contributes to the hydrophobic core. Using NMR titration experiments, we identified residues of the CTD domain involved in the binding to double-stranded DNA. These residues are located on two opposite surfaces at the base of the coiled coil, formed by the N- and C-terminal extremities, where a strictly conserved proline residue induces an overwinding of the coiled coil. Finally, preliminary analysis of NMR spectra recorded on distinct Uup constructs precludes a fully flexible positioning of the CTD domain in full-length Uup. These structural data are the first reported for a non-ATPase domain within ABC REG subfamily. | |||
The C-terminal domain of the Uup protein is a DNA-binding coiled coil motif.,Carlier L, Sander Haase A, Burgos Zepeda MY, Dassa E, Lequin O J Struct Biol. 2012 Sep 17. pii: S1047-8477(12)00247-X. doi:, 10.1016/j.jsb.2012.09.005. PMID:22995754<ref>PMID:22995754</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2lw1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
[[Category: Escherichia coli | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Burgos Zepeda MY]] | ||
[[Category: | [[Category: Carlier L]] | ||
[[Category: Dassa E]] | |||
[[Category: Haase AS]] | |||
[[Category: Lequin O]] | |||