2ius
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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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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[[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 Mon Mar 31 03:48:54 2008'' |
Revision as of 00:48, 31 March 2008
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| , 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
Page seeded by OCA on Mon Mar 31 03:48:54 2008
Categories: 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
