5GUJ

Crystal structure of the Bacillus subtilis DnaG RNA Polymerase Domain, natural degradation of full length DnaG

Summary for 5GUJ

• Entry DOI: 10.2210/pdb5guj/pdb
• Related: 5GUM
• Descriptor: DNA primase (2 entities in total)
• Functional Keywords: transferase
• Biological source: Bacillus subtilis (strain 168)
• Total number of polymer chains: 1
• Total formula weight: 36987.23

Authors

Zhou, Y.,Liu, Z.,Wang, G. (deposition date: 2016-08-29, release date: 2017-04-19, Last modification date: 2023-11-08)

Primary citation

Zhou, Y.,Luo, H.,Liu, Z.,Yang, M.,Pang, X.,Sun, F.,Wang, G.
Structural Insight into the Specific DNA Template Binding to DnaG primase in Bacteria
Sci Rep, 7:659-659, 2017

PubMed Abstract: Bacterial primase initiates the repeated synthesis of short RNA primers that are extended by DNA polymerase to synthesize Okazaki fragments on the lagging strand at replication forks. It remains unclear how the enzyme recognizes specific initiation sites. In this study, the DnaG primase from Bacillus subtilis (BsuDnaG) was characterized and the crystal structure of the RNA polymerase domain (RPD) was determined. Structural comparisons revealed that the tethered zinc binding domain plays an important role in the interactions between primase and specific template sequence. Structural and biochemical data defined the ssDNA template binding surface as an L shape, and a model for the template ssDNA binding to primase is proposed. The flexibility of the DnaG primases from B. subtilis and G. stearothermophilus were compared, and the results implied that the intrinsic flexibility of the primase may facilitate the interactions between primase and various partners in the replisome. These results shed light on the mechanism by which DnaG recognizes the specific initiation site.

PubMed: 28386108
DOI: 10.1038/s41598-017-00767-8

Experimental method

X-RAY DIFFRACTION (2.5 Å)