PMID- 11135672 OWN - NLM STAT- MEDLINE DCOM- 20010118 LR - 20131121 IS - 1072-8368 (Print) IS - 1072-8368 (Linking) VI - 8 IP - 1 DP - 2001 Jan TI - Crystal structure of a DNA-dependent RNA polymerase (DNA primase). PG - 57-61 AB - 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. FAU - Augustin, M A AU - Augustin MA AD - Max-Planck-Institut fur Biochemie, Abteilung fur Strukturforschung, Am Klopferspitz 18A, D-82152 Martinsried, Germany. augustin@biochem.mpg.de FAU - Huber, R AU - Huber R FAU - Kaiser, J T AU - Kaiser JT LA - eng SI - PDB/1G71 PT - Journal Article PL - United States TA - Nat Struct Biol JT - Nature structural biology JID - 9421566 RN - 0 (Protein Subunits) RN - EC 2.7.7.- (DNA Primase) RN - H6241UJ22B (Selenium) RN - J41CSQ7QDS (Zinc) SB - IM CIN - Nat Struct Biol. 2001 Jan;8(1):2-4. PMID: 11135655 MH - Amino Acid Motifs MH - Amino Acid Sequence MH - Binding Sites MH - Catalytic Domain MH - Crystallography, X-Ray MH - DNA Primase/*chemistry/metabolism MH - Models, Molecular MH - Molecular Sequence Data MH - Protein Structure, Secondary MH - Protein Structure, Tertiary MH - Protein Subunits MH - Pyrococcus furiosus/*enzymology MH - Selenium/metabolism MH - Sequence Alignment MH - Sequence Homology, Amino Acid MH - Zinc/metabolism EDAT- 2001/01/03 11:00 MHDA- 2001/02/28 10:01 CRDT- 2001/01/03 11:00 PHST- 2001/01/03 11:00 [pubmed] PHST- 2001/02/28 10:01 [medline] PHST- 2001/01/03 11:00 [entrez] AID - 10.1038/83060 [doi] PST - ppublish SO - Nat Struct Biol. 2001 Jan;8(1):57-61. doi: 10.1038/83060.