期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 300, 期 2, 页码 353-362出版社
ACADEMIC PRESS LTD
DOI: 10.1006/jmbi.2000.3844
关键词
DNA replication; RNA-polymerase; primase; TOPRIM; topoisomerase
资金
- NIGMS NIH HHS [GM38839] Funding Source: Medline
Primases synthesize short RNA strands on single-stranded DNA templates, thereby generating the hybrid duplexes required for the initiation of synthesis by DNA polymerases. We present the crystal structure of the catalytic unit of a primase enzyme, that of a similar to 320 residue fragment of Escherichia coli primase, determined at 2.9 Angstrom resolution. Central to the catalytic unit is a TOPRlM domain that is strikingly similar in its structure to that of corresponding domains in DNA topoisomerases, but is unrelated to the catalytic centers of other DNA or RNA polymerases. The catalytic domain of primase is crescent-shaped, and the concave face of the crescent is predicted to accommodate about 10 base-pairs of RNA-DNA duplex in a loose interaction, thereby limiting processivity. (C) 2000 Academic Press.
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