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2j5o

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Revision as of 18:53, 24 January 2018

Pseudomonas aeruginosa FtsK gamma domain

Structural highlights

2j5o is a 1 chain structure with sequence from "bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2iut, 2iuu, 2j5p
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FTSK_PSEAE] Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Translocation stops specifically at Xer-dif sites, where FtsK interacts with the Xer recombinase, allowing activation of chromosome unlinking by recombination. FtsK orienting polar sequences (KOPS) guide the direction of DNA translocation. FtsK can remove proteins from DNA as it translocates, but translocation stops specifically at XerCD-dif site, thereby preventing removal of XerC and XerD from dif (Probable).^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The bacterial septum-located DNA translocase FtsK coordinates circular chromosome segregation with cell division. Rapid translocation of DNA by FtsK is directed by 8-base-pair DNA motifs (KOPS), so that newly replicated termini are brought together at the developing septum, thereby facilitating completion of chromosome segregation. Translocase functions reside in three domains, alpha, beta and gamma. FtsKalphabeta are necessary and sufficient for ATP hydrolysis-dependent DNA translocation, which is modulated by FtsKgamma through its interaction with KOPS. By solving the FtsKgamma structure by NMR, we show that gamma is a winged-helix domain. NMR chemical shift mapping localizes the DNA-binding site on the gamma domain. Mutated proteins with substitutions in the FtsKgamma DNA-recognition helix are impaired in DNA binding and KOPS recognition, yet remain competent in DNA translocation and XerCD-dif site-specific recombination, which facilitates the late stages of chromosome segregation.

The FtsK gamma domain directs oriented DNA translocation by interacting with KOPS.,Sivanathan V, Allen MD, de Bekker C, Baker R, Arciszewska LK, Freund SM, Bycroft M, Lowe J, Sherratt DJ Nat Struct Mol Biol. 2006 Nov;13(11):965-72. Epub 2006 Oct 22. PMID:17057717^[3]

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

References

↑ Massey TH, Mercogliano CP, Yates J, Sherratt DJ, Lowe J. Double-stranded DNA translocation: structure and mechanism of hexameric FtsK. Mol Cell. 2006 Aug;23(4):457-69. PMID:16916635 doi:10.1016/j.molcel.2006.06.019
↑ Lowe J, Ellonen A, Allen MD, Atkinson C, Sherratt DJ, Grainge I. Molecular mechanism of sequence-directed DNA loading and translocation by FtsK. Mol Cell. 2008 Aug 22;31(4):498-509. PMID:18722176 doi:10.1016/j.molcel.2008.05.027
↑ Sivanathan V, Allen MD, de Bekker C, Baker R, Arciszewska LK, Freund SM, Bycroft M, Lowe J, Sherratt DJ. The FtsK gamma domain directs oriented DNA translocation by interacting with KOPS. Nat Struct Mol Biol. 2006 Nov;13(11):965-72. Epub 2006 Oct 22. PMID:17057717 doi:10.1038/nsmb1158

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2j5o"

@@ Line 3: / Line 3: @@
 <StructureSection load='2j5o' size='340' side='right' caption='[[2j5o]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2j5o]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J5O FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2j5o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J5O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2J5O FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2iut|2iut]], [[2iuu|2iuu]], [[2j5p|2j5p]]</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=2j5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j5o OCA], [http://pdbe.org/2j5o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2j5o RCSB], [http://www.ebi.ac.uk/pdbsum/2j5o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2j5o ProSAT]</span></td></tr>
@@ Line 13: / Line 13: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j5/2j5o_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/j5/2j5o_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2j5o

From Proteopedia

Revision as of 18:53, 24 January 2018

Pseudomonas aeruginosa FtsK gamma domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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