4mzt
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==MazF from S. aureus crystal form II, C2221, 2.3 A== | |
| + | <StructureSection load='4mzt' size='340' side='right'caption='[[4mzt]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4mzt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_N315 Staphylococcus aureus subsp. aureus N315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MZT FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.303Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mzt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mzt OCA], [https://pdbe.org/4mzt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mzt RCSB], [https://www.ebi.ac.uk/pdbsum/4mzt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mzt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MAZF_STAAN MAZF_STAAN] Toxic component of a toxin-antitoxin (TA) module. Ribosome-independent, sequence-specific endoribonuclease that cleaves mRNA, thus inhibiting protein synthesis and inducing bacterial stasis. Cleavages occur preferentially in a U-rich region with a consensus sequence of 5'-[ACG]UU[ACG]-3' in single-stranded RNA (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics.,Zorzini V, Buts L, Sleutel M, Garcia-Pino A, Talavera A, Haesaerts S, Greve HD, Cheung A, van Nuland NA, Loris R Nucleic Acids Res. 2014 Jun 1;42(10):6709-25. doi: 10.1093/nar/gku266. Epub 2014 , Apr 19. PMID:24748664<ref>PMID:24748664</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4mzt" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Staphylococcus aureus subsp. aureus N315]] | ||
| + | [[Category: Cheung A]] | ||
| + | [[Category: Loris R]] | ||
| + | [[Category: Zorzini V]] | ||
| + | [[Category: Van Nuland NAJ]] | ||
Current revision
MazF from S. aureus crystal form II, C2221, 2.3 A
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