3LGB
Crystal Structure of the Fe-S Domain of the yeast DNA primase
Summary for 3LGB
| Entry DOI | 10.2210/pdb3lgb/pdb |
| Descriptor | DNA primase large subunit, IRON/SULFUR CLUSTER, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (6 entities in total) |
| Functional Keywords | dna primase, fe-s cluster, dna-binding, dna-directed rna polymerase, iron, iron-sulfur, metal-binding, nucleotidyltransferase, primosome, transferase |
| Biological source | Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) |
| Total number of polymer chains | 2 |
| Total formula weight | 47289.06 |
| Authors | Sauguet, L.,Pellegrini, L. (deposition date: 2010-01-20, release date: 2010-04-21, Last modification date: 2024-11-13) |
| Primary citation | Sauguet, L.,Klinge, S.,Perera, R.L.,Maman, J.D.,Pellegrini, L. Shared Active Site Architecture between the Large Subunit of Eukaryotic Primase and DNA Photolyase PLOS ONE, 5:10083-10083, 2010 Cited by PubMed Abstract: DNA synthesis during replication relies on RNA primers synthesised by the primase, a specialised DNA-dependent RNA polymerase that can initiate nucleic acid synthesis de novo. In archaeal and eukaryotic organisms, the primase is a heterodimeric enzyme resulting from the constitutive association of a small (PriS) and large (PriL) subunit. The ability of the primase to initiate synthesis of an RNA primer depends on a conserved Fe-S domain at the C-terminus of PriL (PriL-CTD). However, the critical role of the PriL-CTD in the catalytic mechanism of initiation is not understood. PubMed: 20404922DOI: 10.1371/journal.pone.0010083 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.54 Å) |
Structure validation
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