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| | <StructureSection load='2iuu' size='340' side='right'caption='[[2iuu]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='2iuu' size='340' side='right'caption='[[2iuu]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2iuu]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IUU FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2iuu]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IUU FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ius|2ius]], [[2iut|2iut]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></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=2iuu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iuu OCA], [https://pdbe.org/2iuu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iuu RCSB], [https://www.ebi.ac.uk/pdbsum/2iuu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iuu ProSAT]</span></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=2iuu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iuu OCA], [https://pdbe.org/2iuu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iuu RCSB], [https://www.ebi.ac.uk/pdbsum/2iuu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iuu ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/FTSK_PSEAE 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).<ref>PMID:16916635</ref> <ref>PMID:18722176</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lowe, J]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Massey, T H]] | + | [[Category: Lowe J]] |
| - | [[Category: Mercogliano, C P]]
| + | [[Category: Massey TH]] |
| - | [[Category: Sherratt, D J]]
| + | [[Category: Mercogliano CP]] |
| - | [[Category: Yates, J]] | + | [[Category: Sherratt DJ]] |
| - | [[Category: Aaa atpase]] | + | [[Category: Yates J]] |
| - | [[Category: Atp-binding]] | + | |
| - | [[Category: Cell cycle]] | + | |
| - | [[Category: Cell division]]
| + | |
| - | [[Category: Chromosome partition]]
| + | |
| - | [[Category: Divisome]]
| + | |
| - | [[Category: Dna translocation]]
| + | |
| - | [[Category: Dna-binding]]
| + | |
| - | [[Category: Hexameric ring]]
| + | |
| - | [[Category: Inner membrane]]
| + | |
| - | [[Category: Kop]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Nucleotide-binding]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| Structural highlights
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
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[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
- ↑ 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
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