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2ius

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Revision as of 18:41, 10 September 2015

E. COLI FTSK MOTOR DOMAIN

Structural highlights

2ius is a 6 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2iuu, 2iut
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[FTSK_ECOLI] 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. Stoppage of translocation is accompanied by a reduction in ATPase activity. Also stimulates topoisomerase 4 activity. Required for the targeting of FtsQ, FtsL and FtsI to the septum.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9] ^[10] ^[11]

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

FtsK is a DNA translocase that coordinates chromosome segregation and cell division in bacteria. In addition to its role as activator of XerCD site-specific recombination, FtsK can translocate double-stranded DNA (dsDNA) rapidly and directionally and reverse direction. We present crystal structures of the FtsK motor domain monomer, showing that it has a RecA-like core, the FtsK hexamer, and also showing that it is a ring with a large central annulus and a dodecamer consisting of two hexamers, head to head. Electron microscopy (EM) demonstrates the DNA-dependent existence of hexamers in solution and shows that duplex DNA passes through the middle of each ring. Comparison of FtsK monomer structures from two different crystal forms highlights a conformational change that we propose is the structural basis for a rotary inchworm mechanism of DNA translocation.

Double-stranded DNA translocation: structure and mechanism of hexameric FtsK.,Massey TH, Mercogliano CP, Yates J, Sherratt DJ, Lowe J Mol Cell. 2006 Aug;23(4):457-69. PMID:16916635^[12]

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

References

↑ Yu XC, Weihe EK, Margolin W. Role of the C terminus of FtsK in Escherichia coli chromosome segregation. J Bacteriol. 1998 Dec;180(23):6424-8. PMID:9829960
↑ Wang L, Lutkenhaus J. FtsK is an essential cell division protein that is localized to the septum and induced as part of the SOS response. Mol Microbiol. 1998 Aug;29(3):731-40. PMID:9723913
↑ Chen JC, Beckwith J. FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with FtsZ during Escherichia coli cell division. Mol Microbiol. 2001 Oct;42(2):395-413. PMID:11703663
↑ Aussel L, Barre FX, Aroyo M, Stasiak A, Stasiak AZ, Sherratt D. FtsK Is a DNA motor protein that activates chromosome dimer resolution by switching the catalytic state of the XerC and XerD recombinases. Cell. 2002 Jan 25;108(2):195-205. PMID:11832210
↑ Bigot S, Corre J, Louarn JM, Cornet F, Barre FX. FtsK activities in Xer recombination, DNA mobilization and cell division involve overlapping and separate domains of the protein. Mol Microbiol. 2004 Nov;54(4):876-86. PMID:15522074 doi:http://dx.doi.org/10.1111/j.1365-2958.2004.04335.x
↑ Yates J, Zhekov I, Baker R, Eklund B, Sherratt DJ, Arciszewska LK. Dissection of a functional interaction between the DNA translocase, FtsK, and the XerD recombinase. Mol Microbiol. 2006 Mar;59(6):1754-66. PMID:16553881 doi:http://dx.doi.org/10.1111/j.1365-2958.2005.05033.x
↑ Kennedy SP, Chevalier F, Barre FX. Delayed activation of Xer recombination at dif by FtsK during septum assembly in Escherichia coli. Mol Microbiol. 2008 May;68(4):1018-28. doi: 10.1111/j.1365-2958.2008.06212.x., Epub 2008 Mar 19. PMID:18363794 doi:http://dx.doi.org/10.1111/j.1365-2958.2008.06212.x
↑ Bonne L, Bigot S, Chevalier F, Allemand JF, Barre FX. Asymmetric DNA requirements in Xer recombination activation by FtsK. Nucleic Acids Res. 2009 Apr;37(7):2371-80. doi: 10.1093/nar/gkp104. Epub 2009 Feb, 26. PMID:19246541 doi:http://dx.doi.org/10.1093/nar/gkp104
↑ Graham JE, Sivanathan V, Sherratt DJ, Arciszewska LK. FtsK translocation on DNA stops at XerCD-dif. Nucleic Acids Res. 2010 Jan;38(1):72-81. doi: 10.1093/nar/gkp843. Epub 2009 Oct, 23. PMID:19854947 doi:http://dx.doi.org/10.1093/nar/gkp843
↑ Bigot S, Marians KJ. DNA chirality-dependent stimulation of topoisomerase IV activity by the C-terminal AAA+ domain of FtsK. Nucleic Acids Res. 2010 May;38(9):3031-40. doi: 10.1093/nar/gkp1243. Epub 2010, Jan 16. PMID:20081205 doi:http://dx.doi.org/10.1093/nar/gkp1243
↑ Grainge I, Lesterlin C, Sherratt DJ. Activation of XerCD-dif recombination by the FtsK DNA translocase. Nucleic Acids Res. 2011 Jul;39(12):5140-8. doi: 10.1093/nar/gkr078. Epub 2011 Mar, 2. PMID:21371996 doi:http://dx.doi.org/10.1093/nar/gkr078
↑ 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

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/2ius"

@@ Line 2: / Line 2: @@
 <StructureSection load='2ius' size='340' side='right' caption='[[2ius]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ius]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IUS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ius]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IUS FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2iuu|2iuu]], [[2iut|2iut]]</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=2ius FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ius OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ius RCSB], [http://www.ebi.ac.uk/pdbsum/2ius PDBsum]</span></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=2ius FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ius OCA], [http://pdbe.org/2ius PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ius RCSB], [http://www.ebi.ac.uk/pdbsum/2ius PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2ius" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Bacillus coli migula 1895]]
 [[Category: Lowe, J]]
 [[Category: Massey, T H]]

2ius

From Proteopedia

Revision as of 18:41, 10 September 2015

E. COLI FTSK MOTOR DOMAIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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