2ius: Difference between revisions

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[[Image:2ius.~~jpg~~|left|200px]]

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~~'''~~E. COLI FTSK MOTOR DOMAIN~~'''~~

===E. COLI FTSK MOTOR DOMAIN===

~~==Overview==~~

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~~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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_16916635}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16916635 is the PubMed ID number.

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==About this Structure==

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[[Category: Nucleotide-binding]]

[[Category: Transmembrane]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May 4 07~~:54:39 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:06:37 2008''

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-[[Image:2ius.jpg|left|200px]]
+{{Seed}}
+[[Image:2ius.png|left|200px]]
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 {{STRUCTURE_2ius|  PDB=2ius  |  SCENE=  }}
-'''E. COLI FTSK MOTOR DOMAIN'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16916635}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16916635 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16916635}}
 ==About this Structure==
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 [[Category: Nucleotide-binding]]
 [[Category: Transmembrane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 07:54:39 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:06:37 2008''