2mf2

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'''Unreleased structure'''
 
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The entry 2mf2 is ON HOLD until Paper Publication
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==Structural and biophysical characterization of the mRNA interferase SaMazF from Staphylococcus aureus.==
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<StructureSection load='2mf2' size='340' side='right'caption='[[2mf2]]' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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</table>
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== Function ==
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[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]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Zorzini, V., Cheung, A., Loris, R., van Nuland, N.A.J.
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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<ref>PMID:21213075</ref>
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Description: Structural and biophysical characterization of the mRNA interferase SaMazF from Staphylococcus aureus.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2mf2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Staphylococcus aureus]]
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[[Category: Cheung A]]
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[[Category: Loris R]]
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[[Category: Zorzini V]]
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[[Category: Van Nuland NAJ]]

Current revision

Structural and biophysical characterization of the mRNA interferase SaMazF from Staphylococcus aureus.

PDB ID 2mf2

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