Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 4, Issue 1, Pages 55-57Publisher
SPRINGER
DOI: 10.1007/s12104-009-9206-0
Keywords
Prokaryotic zinc finger; NMR resonance assignments; DNA binding protein
Categories
Funding
- Ministero dell'Istruzione, dell'Universita' e della Ricerca [PRIN 2007, FIRB 2003]
- Regione Campania Grant [L.R.5 2006]
Ask authors/readers for more resources
Ml4 protein from Mesorhizobium loti has a 58% sequence identity with the Ros protein from Agrobacterium tumefaciens that contains a prokaryotic Cys(2)His(2) zinc finger domain. Interestingly, Ml4 is a zinc-lacking protein that does not contain the Cys(2)His(2) motif and is able to bind the Ros DNA target sequence with high affinity. Here we report the H-1, N-15 and C-13 NMR assignments of the Ml4 protein DNA binding domain (residue 52-151), as an important step toward elucidating at a molecular level how this prokaryotic domain can overcome the metal requirement for proper folding and DNA-binding activity.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available