Structural highlights
Function
LOADL_BPT4 Forms the sliding-clamp-loader together with the small subunit (PubMed:10585481). Functions as an ATPase enzyme (PubMed:16800623, PubMed:18676368). The clamp loader holds the clamp in an open conformation and places it onto the DNA (PubMed:22194570, PubMed:18676368). 4 ATP molecules must bind to the sliding-clamp-loader before the latter can open the sliding clamp (PubMed:18676368). ATP hydrolysis triggers the detachment of the sliding clamp from the sliding-clamp-loader, freeing the sliding clamp to track along DNA (PubMed:18676368, PubMed:22194570).[HAMAP-Rule:MF_04162][1] [2] [3] [4]
References
- ↑ Janzen DM, Torgov MY, Reddy MK. In vitro reconstitution of the bacteriophage T4 clamp loader complex (gp44/62). J Biol Chem. 1999 Dec 10;274(50):35938-43. PMID:10585481 doi:10.1074/jbc.274.50.35938
- ↑ Zhuang Z, Berdis AJ, Benkovic SJ. An alternative clamp loading pathway via the T4 clamp loader gp44/62-DNA complex. Biochemistry. 2006 Jul 4;45(26):7976-89. PMID:16800623 doi:http://dx.doi.org/10.1021/bi0601205
- ↑ Pietroni P, von Hippel PH. Multiple ATP binding is required to stabilize the "activated" (clamp open) clamp loader of the T4 DNA replication complex. J Biol Chem. 2008 Oct 17;283(42):28338-53. doi: 10.1074/jbc.M804371200. Epub 2008, Aug 1. PMID:18676368 doi:http://dx.doi.org/10.1074/jbc.M804371200
- ↑ Kelch BA, Makino DL, O'Donnell M, Kuriyan J. How a DNA polymerase clamp loader opens a sliding clamp. Science. 2011 Dec 23;334(6063):1675-80. PMID:22194570 doi:10.1126/science.1211884
