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TitleStructural and Molecular Basis for Coordination in a Viral DNA Packaging Motor.
Journal, issue, pagesCell Rep, Vol. 14, Issue 8, Page 2017-2029, Year 2016
Publish dateMar 1, 2016
AuthorsHuzhang Mao / Mitul Saha / Emilio Reyes-Aldrete / Michael B Sherman / Michael Woodson / Rockney Atz / Shelley Grimes / Paul J Jardine / Marc C Morais /
PubMed AbstractRing NTPases are a class of ubiquitous molecular motors involved in basic biological partitioning processes. dsDNA viruses encode ring ATPases that translocate their genomes to near-crystalline ...Ring NTPases are a class of ubiquitous molecular motors involved in basic biological partitioning processes. dsDNA viruses encode ring ATPases that translocate their genomes to near-crystalline densities within pre-assembled viral capsids. Here, X-ray crystallography, cryoEM, and biochemical analyses of the dsDNA packaging motor in bacteriophage phi29 show how individual subunits are arranged in a pentameric ATPase ring and suggest how their activities are coordinated to translocate dsDNA. The resulting pseudo-atomic structure of the motor and accompanying functional analyses show how ATP is bound in the ATPase active site; identify two DNA contacts, including a potential DNA translocating loop; demonstrate that a trans-acting arginine finger is involved in coordinating hydrolysis around the ring; and suggest a functional coupling between the arginine finger and the DNA translocating loop. The ability to visualize the motor in action illuminates how the different motor components interact with each other and with their DNA substrate.
External linksCell Rep / PubMed:26904950 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.941 - 12.0 Å
Structure data

EMDB-6560:
Bacteriophage phi29 prohead particle stalled during DNA packaging
Method: EM (single particle) / Resolution: 12.0 Å

PDB-5hd9:
Crystal Structure of the N-terminal domain of the DNA packaging ATPase from bacteriophage phi29
Method: X-RAY DIFFRACTION / Resolution: 1.941 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • bacillus phage phi29 (virus)
KeywordsVIRAL PROTEIN / ASCE fold

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