DnaC helicase loader

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{{STRUCTURE_2vye| PDB=2vye | SIZE=400| SCENE= |right|CAPTION=DnaC helicase loader dimer part of hexamer complex with DNA [[2vye]] }}
{{STRUCTURE_2vye| PDB=2vye | SIZE=400| SCENE= |right|CAPTION=DnaC helicase loader dimer part of hexamer complex with DNA [[2vye]] }}
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'''DnaC helicase loader''' (DnaC) transfers helicase to replication origins. The helicase loaders belong to two classes. The ‘ring breakers’ break the hexameric helicase to allow the DNA to pass through. The ‘ring makers’ assemble the helicase monomers to hexamers around the DNA.
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'''DnaC helicase loader''' (DnaC) transfers helicase to replication origins. The helicase loaders belong to two classes. The ‘'''ring breakers'''’ break the hexameric helicase to allow the DNA to pass through. The ‘'''ring makers'''’ assemble the helicase monomers to hexamers around the DNA.<ref>PMID:23562643</ref>
For the theoretical model structure of E. coli DnaC see [[Structure of E. coli DnaC helicase loader]].
For the theoretical model structure of E. coli DnaC see [[Structure of E. coli DnaC helicase loader]].
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[[2vyf]] – GkDnaC
[[2vyf]] – GkDnaC
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 12:41, 3 January 2016

Template:STRUCTURE 2vye

DnaC helicase loader (DnaC) transfers helicase to replication origins. The helicase loaders belong to two classes. The ‘ring breakers’ break the hexameric helicase to allow the DNA to pass through. The ‘ring makers’ assemble the helicase monomers to hexamers around the DNA.[1]

For the theoretical model structure of E. coli DnaC see Structure of E. coli DnaC helicase loader.

3D Structures of DnaC helicase loader

Updated on 03-January-2016

3ec2 – AaDnaC – Aquifex aeolicus
3ecc – AaDnaC + ADP-BeF3
2vye – GkDnaC + DNA – Geobacillus kaustophilus
2vyf – GkDnaC

References

  1. ↑ Arias-Palomo E, O'Shea VL, Hood IV, Berger JM. The bacterial DnaC helicase loader is a DnaB ring breaker. Cell. 2013 Apr 11;153(2):438-48. doi: 10.1016/j.cell.2013.03.006. Epub 2013 Apr, 4. PMID:23562643 doi:http://dx.doi.org/10.1016/j.cell.2013.03.006

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Eric Martz

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