3U60

Structure of T4 Bacteriophage Clamp Loader Bound To Open Clamp, DNA and ATP Analog

Summary for 3U60

• Entry DOI: 10.2210/pdb3u60/pdb
• Related: 1CZD 1JR3 1SXJ 1XXH 3GLF 3U5Z 3U61
• Descriptor: DNA polymerase accessory protein 44, Template DNA strand, Primer DNA strand, ... (8 entities in total)
• Functional Keywords: aaa+, atp hydrolase, sliding clamp, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Enterobacteria phage T4; More
• Total number of polymer chains: 10
• Total formula weight: 259944.82

Authors

Kelch, B.A.,Makino, D.L.,O'Donnell, M.,Kuriyan, J. (deposition date: 2011-10-11, release date: 2012-01-04, Last modification date: 2024-11-06)

Primary citation

Kelch, B.A.,Makino, D.L.,O'Donnell, M.,Kuriyan, J.
How a DNA polymerase clamp loader opens a sliding clamp.
Science, 334:1675-1680, 2011

PubMed Abstract: Processive chromosomal replication relies on sliding DNA clamps, which are loaded onto DNA by pentameric clamp loader complexes belonging to the AAA+ family of adenosine triphosphatases (ATPases). We present structures for the ATP-bound state of the clamp loader complex from bacteriophage T4, bound to an open clamp and primer-template DNA. The clamp loader traps a spiral conformation of the open clamp so that both the loader and the clamp match the helical symmetry of DNA. One structure reveals that ATP has been hydrolyzed in one subunit and suggests that clamp closure and ejection of the loader involves disruption of the ATP-dependent match in symmetry. The structures explain how synergy among the loader, the clamp, and DNA can trigger ATP hydrolysis and release of the closed clamp on DNA.

PubMed: 22194570
DOI: 10.1126/science.1211884

Experimental method

X-RAY DIFFRACTION (3.34 Å)