2lw1: Difference between revisions

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[[~~Image~~:2lw1.~~png|left|200px~~]]

==The C-terminal domain of the Uup protein is a DNA-binding coiled coil motif==

== Structural highlights ==

<table><tr><td colspan='2'>[[2lw1]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LW1 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uup, ycbH, ycbI, b0949, JW0932 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lw1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lw1 RCSB], [http://www.ebi.ac.uk/pdbsum/2lw1 PDBsum]</span></td></tr>

<table>

== 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.

~~{{STRUCTURE_2lw1| PDB=2lw1 | SCENE= }}~~

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>

~~===The C-terminal domain~~ of the ~~Uup protein is a DNA-binding coiled coil motif===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_22995754}}~~

== References ==

==~~About this Structure~~==

__TOC__

~~[[2lw1]] is a 1 chain structure with sequence from [http:~~//~~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].~~

</StructureSection>

[[Category: Escherichia coli k-12]]

[[Category: Carlier, L.]]

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@@ Line 1: / Line 1: @@
-[[Image:2lw1.png|left|200px]]
+==The C-terminal domain of the Uup protein is a DNA-binding coiled coil motif==
+<StructureSection load='2lw1' size='340' side='right' caption='[[2lw1]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2lw1]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LW1 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uup, ycbH, ycbI, b0949, JW0932 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lw1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lw1 RCSB], [http://www.ebi.ac.uk/pdbsum/2lw1 PDBsum]</span></td></tr>
+<table>
+<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.
-{{STRUCTURE_2lw1|  PDB=2lw1  |  SCENE=  }}
+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>
-===The C-terminal domain of the Uup protein is a DNA-binding coiled coil motif===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_22995754}}
+== References ==
+<references/>
-==About this Structure==
+__TOC__
-[[2lw1]] is a 1 chain structure with sequence from [http://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].
+</StructureSection>
 [[Category: Escherichia coli k-12]]
 [[Category: Carlier, L.]]