2iuu: Difference between revisions
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==Overview== | ==Overview== | ||
FtsK is a DNA translocase that coordinates chromosome segregation and cell | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Lowe, J.]] | [[Category: Lowe, J.]] | ||
[[Category: Massey, T | [[Category: Massey, T H.]] | ||
[[Category: Mercogliano, C | [[Category: Mercogliano, C P.]] | ||
[[Category: Sherratt, D | [[Category: Sherratt, D J.]] | ||
[[Category: Yates, J.]] | [[Category: Yates, J.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:13 2008'' | ||
Revision as of 15:56, 21 February 2008
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P. AERUGINOSA FTSK MOTOR DOMAIN, HEXAMER
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
2IUU is a Single protein structure of sequence from Pseudomonas aeruginosa with ADP as ligand. Known structural/functional Site: AC1. 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
Page seeded by OCA on Thu Feb 21 17:56:13 2008
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Pseudomonas aeruginosa
- Single protein
- Lowe, J.
- Massey, T H.
- Mercogliano, C P.
- Sherratt, D J.
- Yates, J.
- ADP
- Aaa atpase
- Atp-binding
- Cell cycle
- Cell division
- Chromosome partition
- Divisome
- Dna translocation
- Dna-binding
- Hexameric ring
- Inner membrane
- Kops
- Membrane
- Membrane protein
- Nucleotide-binding
- Transmembrane
