2MF2
Structural and biophysical characterization of the mRNA interferase SaMazF from Staphylococcus aureus.
Summary for 2MF2
| Entry DOI | 10.2210/pdb2mf2/pdb |
| Related | 4MZM 4MZP 4MZT |
| NMR Information | BMRB: 17288 |
| Descriptor | mRNA interferase MazF (1 entity in total) |
| Functional Keywords | ccdb/mazf fold, ribonuclease, hydrolase |
| Biological source | Staphylococcus aureus (Staphylococcus aureus) |
| Total number of polymer chains | 2 |
| Total formula weight | 29642.02 |
| Authors | Zorzini, V.,Cheung, A.,Loris, R.,van Nuland, N.A.J. (deposition date: 2013-10-03, release date: 2014-05-21, Last modification date: 2024-05-15) |
| Primary citation | Zorzini, V.,Buts, L.,Sleutel, M.,Garcia-Pino, A.,Talavera, A.,Haesaerts, S.,De Greve, H.,Cheung, A.,van Nuland, N.A.J.,Loris, R. Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics Nucleic Acids Res., 5:157-160, 2014 Cited by PubMed Abstract: MazF proteins are ribonucleases that cleave mRNA with high sequence-specificity as part of bacterial stress response and that are neutralized by the action of the corresponding antitoxin MazE. Prolonged activation of the toxin MazF leads to cell death. Several mazEF modules from gram-negative bacteria have been characterized in terms of catalytic activity, auto-regulation mechanism and structure, but less is known about their distant relatives found in gram-positive organisms. Currently, no solution NMR structure is available for any wild-type MazF toxin. Here we report the (1)H, (15)N and (13)C backbone and side-chain chemical shift assignments of this toxin from the pathogen bacterium Staphylococcus aureus. The BMRB accession number is 17288. PubMed: 21213075DOI: 10.1007/s12104-010-9290-1 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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