1DD9

STRUCTURE OF THE DNAG CATALYTIC CORE

Summary for 1DD9

Entry DOI	10.2210/pdb1dd9/pdb
Related	1DDE
Descriptor	DNA PRIMASE, STRONTIUM 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	38309.87
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.6 Å)

Structure validation