2ius: Difference between revisions

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New page: left|200px<br /><applet load="2ius" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ius, resolution 2.7Å" /> '''E. COLI FTSK MOTOR DO...
 
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[[Image:2ius.jpg|left|200px]]<br /><applet load="2ius" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2ius, resolution 2.7&Aring;" />
caption="2ius, resolution 2.7&Aring;" />
'''E. COLI FTSK MOTOR DOMAIN'''<br />
'''E. COLI FTSK MOTOR DOMAIN'''<br />


==Overview==
==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.
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==
2IUS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IUS OCA].  
2IUS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Lowe, J.]]
[[Category: Lowe, J.]]
[[Category: Massey, T.H.]]
[[Category: Massey, T H.]]
[[Category: Mercogliano, C.P.]]
[[Category: Mercogliano, C P.]]
[[Category: Sherratt, D.J.]]
[[Category: Sherratt, D J.]]
[[Category: Yates, J.]]
[[Category: Yates, J.]]
[[Category: aaa atpase]]
[[Category: aaa atpase]]
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[[Category: transmembrane]]
[[Category: transmembrane]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:33:17 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:14 2008''

Revision as of 18:56, 21 February 2008

File:2ius.jpg


2ius, resolution 2.7Å

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E. COLI FTSK MOTOR DOMAIN

OverviewOverview

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 StructureAbout this Structure

2IUS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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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