1G71

CRYSTAL STRUCTURE OF PYROCOCCUS FURIOSUS DNA PRIMASE

Summary for 1G71

• Entry DOI: 10.2210/pdb1g71/pdb
• Related: 1DD9 1DDE 1EQN
• Descriptor: DNA PRIMASE, ZINC ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: zinc-knuckle, replication
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 2
• Total formula weight: 82409.84

Authors

Augustin, M.A.,Huber, R.,Kaiser, J.T. (deposition date: 2000-11-08, release date: 2001-01-10, Last modification date: 2024-02-07)

Primary citation

Augustin, M.A.,Huber, R.,Kaiser, J.T.
Crystal structure of a DNA-dependent RNA polymerase (DNA primase).
Nat.Struct.Biol., 8:57-61, 2001

PubMed Abstract: Primases are essential components of the DNA replication apparatus in every organism. They catalyze the synthesis of oligoribonucleotides on single-stranded DNA, which subsequently serve as primers for the replicative DNA polymerases. In contrast to bacterial primases, the archaeal enzymes are closely related to their eukaryotic counterparts. We have solved the crystal structure of the catalytic primase subunit from the hyperthermophilic archaeon Pyrococcus furiosus at 2.3 A resolution by multiwavelength anomalous dispersion methods. The structure shows a two-domain arrangement with a novel zinc knuckle motif located in the primase (prim) domain. In this first structure of a complete protein of the archaeal/eukaryotic primase family, the arrangement of the catalytically active residues resembles the active sites of various DNA polymerases that are unrelated in fold.

PubMed: 11135672
DOI: 10.1038/83060

Experimental method

X-RAY DIFFRACTION (2.3 Å)