6N7W
Structure of bacteriophage T7 leading-strand DNA polymerase (D5A/E7A)/Trx in complex with a DNA fork and incoming dTTP (from multiple lead complexes)
Summary for 6N7W
| Entry DOI | 10.2210/pdb6n7w/pdb |
| EMDB information | 0357 0359 0362 0363 0364 0365 |
| Descriptor | DNA-directed DNA polymerase, TrxA, DNA (25-MER), ... (6 entities in total) |
| Functional Keywords | dna polymerase, helicase, dna replication, replisome, transferase-dna complex, transferase/dna |
| Biological source | Enterobacteria phage T7 (Bacteriophage T7) More |
| Total number of polymer chains | 4 |
| Total formula weight | 123125.53 |
| Authors | |
| Primary citation | Gao, Y.,Cui, Y.,Fox, T.,Lin, S.,Wang, H.,de Val, N.,Zhou, Z.H.,Yang, W. Structures and operating principles of the replisome. Science, 363:-, 2019 Cited by PubMed Abstract: Visualization in atomic detail of the replisome that performs concerted leading- and lagging-DNA strand synthesis at a replication fork has not been reported. Using bacteriophage T7 as a model system, we determined cryo-electron microscopy structures up to 3.2-angstroms resolution of helicase translocating along DNA and of helicase-polymerase-primase complexes engaging in synthesis of both DNA strands. Each domain of the spiral-shaped hexameric helicase translocates sequentially hand-over-hand along a single-stranded DNA coil, akin to the way AAA+ ATPases (adenosine triphosphatases) unfold peptides. Two lagging-strand polymerases are attached to the primase, ready for Okazaki fragment synthesis in tandem. A β hairpin from the leading-strand polymerase separates two parental DNA strands into a T-shaped fork, thus enabling the closely coupled helicase to advance perpendicular to the downstream DNA duplex. These structures reveal the molecular organization and operating principles of a replisome. PubMed: 30679383DOI: 10.1126/science.aav7003 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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