5I7M
Crystal structure of Y345F mutant of human primase p58 iron-sulfur cluster domain
Summary for 5I7M
| Entry DOI | 10.2210/pdb5i7m/pdb |
| Descriptor | DNA primase large subunit, IRON/SULFUR CLUSTER, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | dna replication, primase, [4fe-4s], p58c, replication |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 2 |
| Total formula weight | 44219.08 |
| Authors | Salay, L.E.,Thompson, M.K.,Chazin, W.J. (deposition date: 2016-02-17, release date: 2017-03-01, Last modification date: 2024-10-09) |
| Primary citation | O'Brien, E.,Holt, M.E.,Thompson, M.K.,Salay, L.E.,Ehlinger, A.C.,Chazin, W.J.,Barton, J.K. The [4Fe4S] cluster of human DNA primase functions as a redox switch using DNA charge transport. Science, 355:-, 2017 Cited by PubMed Abstract: DNA charge transport chemistry offers a means of long-range, rapid redox signaling. We demonstrate that the [4Fe4S] cluster in human DNA primase can make use of this chemistry to coordinate the first steps of DNA synthesis. Using DNA electrochemistry, we found that a change in oxidation state of the [4Fe4S] cluster acts as a switch for DNA binding. Single-atom mutations that inhibit this charge transfer hinder primase initiation without affecting primase structure or polymerization. Generating a single base mismatch in the growing primer duplex, which attenuates DNA charge transport, inhibits primer truncation. Thus, redox signaling by [4Fe4S] clusters using DNA charge transport regulates primase binding to DNA and illustrates chemistry that may efficiently drive substrate handoff between polymerases during DNA replication. PubMed: 28232525DOI: 10.1126/science.aag1789 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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