1H, 13C, and 15N NMR assignments for the helicase interaction domain of Staphylococcus aureus DnaG primase

被引：0
作者：
Matthew D. Shortridge
Mark A. Griep
Robert Powers
机构：
[1] University of Nebraska-Lincoln,Department of Chemistry
[2] University of Nebraska-Lincoln,Department of Chemistry
[3] University of Nebraska-Lincoln,Department of Chemistry
来源：
Biomolecular NMR Assignments | 2012年 / 6卷
关键词：
DnaG; Primase; Helicase; NMR; Resonance assignments;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
The interaction between DnaG primase and DnaB helicase is essential for stimulating primer synthesis during bacterial DNA replication. The interaction occurs between the N-terminal domain of helicase and the C-terminal domain of primase. Here we present the 1H, 13C, and 15N backbone and side-chain resonance assignments for the C-terminal helicase interaction domain of Staphylococcus aureus primase.
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页码：35 / 38
页数：3
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