2ius: Difference between revisions
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|RESOURCES=<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.ebi.ac.uk/pdbsum/2ius PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ius RCSB]</span> | |||
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:48:54 2008'' | ||
Revision as of 00:48, 31 March 2008
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| 2ius, resolution 2.7Å | |||||||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
E. COLI FTSK MOTOR DOMAIN
Overview
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.
About this Structure
2IUS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Escherichia coli
- Single protein
- Lowe, J.
- Massey, T H.
- Mercogliano, C P.
- Sherratt, D J.
- Yates, J.
- Aaa atpase
- Atp-binding
- Cell cycle
- Cell division
- Chromosome partition
- Divisome
- Dna translocation
- Dna-binding
- Hexameric ring
- Inner membrane
- Kop
- Membrane
- Membrane protein
- Nucleotide-binding
- Transmembrane