4MZM
MazF from S. aureus crystal form I, P212121, 2.1 A
Summary for 4MZM
| Entry DOI | 10.2210/pdb4mzm/pdb |
| Related | 2MF2 4MZP 4MZT |
| Descriptor | mRNA interferase MazF (2 entities in total) |
| Functional Keywords | ccdb/mazf fold, ribonuclease, maze, mrna interferase, hydrolase |
| Biological source | Staphylococcus aureus subsp. aureus |
| Total number of polymer chains | 4 |
| Total formula weight | 59808.82 |
| Authors | Zorzini, V.,Loris, R.,van Nuland, N.A.J.,Cheung, A. (deposition date: 2013-09-30, release date: 2014-05-28, Last modification date: 2023-09-20) |
| Primary citation | Zorzini, V.,Buts, L.,Sleutel, M.,Garcia-Pino, A.,Talavera, A.,Haesaerts, S.,Greve, H.D.,Cheung, A.,van Nuland, N.A.,Loris, R. Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics. Nucleic Acids Res., 42:6709-6725, 2014 Cited by PubMed Abstract: The Staphylococcus aureus genome contains three toxin-antitoxin modules, including one mazEF module, SamazEF. Using an on-column separation protocol we are able to obtain large amounts of wild-type SaMazF toxin. The protein is well-folded and highly resistant against thermal unfolding but aggregates at elevated temperatures. Crystallographic and nuclear magnetic resonance (NMR) solution studies show a well-defined dimer. Differences in structure and dynamics between the X-ray and NMR structural ensembles are found in three loop regions, two of which undergo motions that are of functional relevance. The same segments also show functionally relevant dynamics in the distantly related CcdB family despite divergence of function. NMR chemical shift mapping and analysis of residue conservation in the MazF family suggests a conserved mode for the inhibition of MazF by MazE. PubMed: 24748664DOI: 10.1093/nar/gku266 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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