1DDE

STRUCTURE OF THE DNAG CATALYTIC CORE

Summary for 1DDE

• Entry DOI: 10.2210/pdb1dde/pdb
• Related: 1DD9
• Descriptor: DNA PRIMASE, YTTRIUM ION (3 entities in total)
• Functional Keywords: toprim, 3-helix bundle, dna-binding protein, rna polymerase, replication protein, primase, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 38577.88

Authors

Keck, J.L.,Roche, D.D.,Lynch, A.S.,Berger, J.M. (deposition date: 1999-11-09, release date: 2000-04-07, Last modification date: 2024-02-07)

Primary citation

Keck, J.L.,Roche, D.D.,Lynch, A.S.,Berger, J.M.
Structure of the RNA polymerase domain of E. coli primase.
Science, 287:2482-2486, 2000

PubMed Abstract: All cellular organisms use specialized RNA polymerases called "primases" to synthesize RNA primers for the initiation of DNA replication. The high-resolution crystal structure of a primase, comprising the catalytic core of the Escherichia coli DnaG protein, was determined. The core structure contains an active-site architecture that is unrelated to other DNA or RNA polymerase palm folds, but is instead related to the "toprim" fold. On the basis of the structure, it is likely that DnaG binds nucleic acid in a groove clustered with invariant residues and that DnaG is positioned within the replisome to accept single-stranded DNA directly from the replicative helicase.

PubMed: 10741967
DOI: 10.1126/science.287.5462.2482

Experimental method

X-RAY DIFFRACTION (1.7 Å)