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TitleNucleotide and partner-protein control of bacterial replicative helicase structure and function.
Journal, issue, pagesMol Cell, Vol. 52, Issue 6, Page 844-854, Year 2013
Publish dateDec 26, 2013
AuthorsMelania S Strycharska / Ernesto Arias-Palomo / Artem Y Lyubimov / Jan P Erzberger / Valerie L O'Shea / Carlos J Bustamante / James M Berger /
PubMed AbstractCellular replication forks are powered by ring-shaped, hexameric helicases that encircle and unwind DNA. To better understand the molecular mechanisms and control of these enzymes, we used multiple ...Cellular replication forks are powered by ring-shaped, hexameric helicases that encircle and unwind DNA. To better understand the molecular mechanisms and control of these enzymes, we used multiple methods to investigate the bacterial replicative helicase, DnaB. A 3.3 Å crystal structure of Aquifex aeolicus DnaB, complexed with nucleotide, reveals a newly discovered conformational state for this motor protein. Electron microscopy and small angle X-ray scattering studies confirm the state seen crystallographically, showing that the DnaB ATPase domains and an associated N-terminal collar transition between two physical states in a nucleotide-dependent manner. Mutant helicases locked in either collar state are active but display different capacities to support critical activities such as duplex translocation and primase-dependent RNA synthesis. Our findings establish the DnaB collar as an autoregulatory hub that controls the ability of the helicase to transition between different functional states in response to both nucleotide and replication initiation/elongation factors.
External linksMol Cell / PubMed:24373746 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.301 - 23.0 Å
Structure data

EMDB-2508:
Nucleotide and partner-protein control of bacterial replicative helicase structure and function
Method: EM (single particle) / Resolution: 23.0 Å

PDB-4nmn:
Aquifex aeolicus replicative helicase (DnaB) complexed with ADP, at 3.3 resolution
Method: X-RAY DIFFRACTION / Resolution: 3.301 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-SR:
STRONTIUM ION

ChemComp-HOH:
WATER

Source
  • aquifex aeolicus (bacteria)
KeywordsREPLICATION / RecA-type helicase / Replicative DNA helicase / ATP binding / DNA-binding

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