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| | ==Structural and biophysical characterization of the mRNA interferase SaMazF from Staphylococcus aureus.== | | ==Structural and biophysical characterization of the mRNA interferase SaMazF from Staphylococcus aureus.== |
| - | <StructureSection load='2mf2' size='340' side='right' caption='[[2mf2]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2mf2' size='340' side='right'caption='[[2mf2]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mf2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MF2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mf2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MF2 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mzm|4mzm]], [[4mzt|4mzt]], [[4mzp|4mzp]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mazF, MW1992 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=2mf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mf2 OCA], [https://pdbe.org/2mf2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mf2 RCSB], [https://www.ebi.ac.uk/pdbsum/2mf2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mf2 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mf2 OCA], [http://pdbe.org/2mf2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mf2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mf2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mf2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MAZF_STAAW MAZF_STAAW]] 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). | + | [https://www.uniprot.org/uniprot/MAZF_STAA8 MAZF_STAA8] Toxic component of a type II toxin-antitoxin (TA) system. Ribosome-independent, sequence-specific endoribonuclease that cleaves mRNA, thus inhibiting protein synthesis and inducing bacterial stasis. It cuts between the first and nucleotides of 5'-UACAU-3' in single-stranded RNA. Neutralized by coexpression with cognate antitoxin MazE.[UniProtKB:A6QIR4] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cheung, A]] | + | [[Category: Large Structures]] |
| - | [[Category: Loris, R]] | + | [[Category: Staphylococcus aureus]] |
| - | [[Category: Nuland, N A.J van]] | + | [[Category: Cheung A]] |
| - | [[Category: Zorzini, V]] | + | [[Category: Loris R]] |
| - | [[Category: Ccdb/mazf fold]] | + | [[Category: Zorzini V]] |
| - | [[Category: Hydrolase]] | + | [[Category: Van Nuland NAJ]] |
| - | [[Category: Ribonuclease]]
| + | |
| Structural highlights
Function
MAZF_STAA8 Toxic component of a type II toxin-antitoxin (TA) system. Ribosome-independent, sequence-specific endoribonuclease that cleaves mRNA, thus inhibiting protein synthesis and inducing bacterial stasis. It cuts between the first and nucleotides of 5'-UACAU-3' in single-stranded RNA. Neutralized by coexpression with cognate antitoxin MazE.[UniProtKB:A6QIR4]
Publication Abstract from PubMed
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.
1H, 13C, and 15N backbone and side-chain chemical shift assignment of the staphylococcal MazF mRNA interferase.,Zorzini V, Haesaerts S, Cheung A, Loris R, van Nuland NA Biomol NMR Assign. 2011 Oct;5(2):157-60. doi: 10.1007/s12104-010-9290-1. Epub, 2011 Jan 7. PMID:21213075[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zorzini V, Haesaerts S, Cheung A, Loris R, van Nuland NA. 1H, 13C, and 15N backbone and side-chain chemical shift assignment of the staphylococcal MazF mRNA interferase. Biomol NMR Assign. 2011 Oct;5(2):157-60. doi: 10.1007/s12104-010-9290-1. Epub, 2011 Jan 7. PMID:21213075 doi:http://dx.doi.org/10.1007/s12104-010-9290-1
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