Assignment of 1H, 13C and 15N resonances of N-terminal domain of DnaA protein

Yoshito Abe; Noriko Watanabe; Yuichiro Yoshida; Fumi Ebata; Tsutomu Katayama; Tadashi Ueda

doi:10.1007/s12104-007-9015-2

Assignment of 1H, 13C and 15N resonances of N-terminal domain of DnaA protein

Biomol NMR Assign. 2007 Jul;1(1):57-9. doi: 10.1007/s12104-007-9015-2. Epub 2007 May 5.

Authors

Yoshito Abe¹, Noriko Watanabe, Yuichiro Yoshida, Fumi Ebata, Tsutomu Katayama, Tadashi Ueda

Affiliation

¹ Department of Immunology, Graduate School of Pharmaceutical Sciences, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.

PMID: 19636826
DOI: 10.1007/s12104-007-9015-2

Abstract

DnaA protein is a key protein in the initiation of chromosomal replication in Escherichia coli. We reported the assignments of 1H, 13C, and 15N resonances of N-terminal domain of Dna A (1-108) which contains the activities of self-oligomerization and DnaB helicase loading.

MeSH terms

Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Bacterial Proteins / metabolism
Binding Sites
DNA Replication
DNA-Binding Proteins / chemistry*
DNA-Binding Proteins / genetics
DNA-Binding Proteins / metabolism
Escherichia coli Proteins / chemistry*
Escherichia coli Proteins / genetics
Escherichia coli Proteins / metabolism
Nuclear Magnetic Resonance, Biomolecular
Peptide Fragments / chemistry
Peptide Fragments / genetics
Protein Structure, Tertiary
Recombinant Proteins / chemistry
Recombinant Proteins / genetics

Substances

Bacterial Proteins
DNA-Binding Proteins
DnaA protein, Bacteria
Escherichia coli Proteins
Peptide Fragments
Recombinant Proteins