3u5z | pdb_00003u5z

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Structure of T4 Bacteriophage clamp loader bound to the T4 clamp, primer-template DNA, and ATP analog

spinqualitylabelsall models 3u5z, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3u5z is a 20 chain structure with sequence from Bpt4. The June 2012 RCSB PDB Molecule of the Month feature on Sliding Clamps by David Goodsell is 10.2210/rcsb_pdb/mom_2012_6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 08T, ADP, MG NonStd Res: MSE Related: 1czd, 1sxj, 3glf, 1jr3, 1xxh, 3u60, 3u61 Gene: 44, gp44 (BPT4), 62, gp62 (BPT4), 45, gp45 (BPT4) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Warning: this is a large structure, and loading might take a long time or not happen at all. Function [DPA44_BPT4] Function as a sliding-clamp-loading ATPase enzyme during DNA replication. Required for elongation of primed templates by controlling the polymerase processivity. Possesses DNA-dependent ATPase activity on its own and within the heterodimer gp44/gp62. Progressive binding of ATPs triggers a conformational change in the complex that inhibits ATPase activity. [DPA5_BPT4] Replisome sliding clamp subunit. Responsible for tethering the catalytic subunit of DNA polymerase to DNA during high-speed replication. [DPA62_BPT4] Function as a sliding-clamp-loading ATPase enzyme during DNA replication. Required for elongation of primed templates by controlling the polymerase processivity. Progressive binding of ATPs triggers a conformational change in the complex that inhibits ATPase activity. Publication Abstract from PubMed 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. How a DNA polymerase clamp loader opens a sliding clamp.,Kelch BA, Makino DL, O'Donnell M, Kuriyan J Science. 2011 Dec 23;334(6063):1675-80. PMID:22194570 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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