7d2n

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'''Unreleased structure'''
 
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The entry 7d2n is ON HOLD until Paper Publication
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==Crystal structure of MazE-MazF (Form-III) from Deinococcus radiodurans==
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<StructureSection load='7d2n' size='340' side='right'caption='[[7d2n]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7d2n]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7D2N 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">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</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=7d2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d2n OCA], [https://pdbe.org/7d2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7d2n RCSB], [https://www.ebi.ac.uk/pdbsum/7d2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7d2n ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q9RX98_DEIRA Q9RX98_DEIRA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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In prokaryotes, toxin-antitoxin (TA) systems are commonly found. They likely reflect the adaptation of pathogenic bacteria or extremophiles to various unfavorable environments by slowing their growth rate. Genomic analysis of the extremophile Deinococcus radiodurans R1 revealed the presence of eight type II TA systems, including the genes dr0417, dr0660, dr1530, dr0690, and dr1807. Expression of these toxin genes led to inhibition of Escherichia coli growth, whereas their antidote antitoxins were able to recover the growth defect. Remarkably, Dr0417 (DrMazF) showed endoribonuclease activity toward rRNAs as well as mRNAs, as determined by in vivo and in vitro RNA cleavage assays, and this activity was inhibited by Dr0416 (DrMazE). It was also found that the expression of dr0416-0417 module is directly regulated by the DrMazE-MazF complex. Furthermore, this TA module was induced under stress conditions and plays an important role in survival. To understand the regulatory mechanism at the molecular level, we determined the first high-resolution structures of DrMazF alone and of the DrMazE-MazF complex. In contrast with the hetero-hexameric state of typical MazE-MazF complexes found in other species, DrMazE-MazF crystal structure consists of a hetero-trimer, with the DNA-binding domain of DrMazE undergoing self-cleavage at the flexible linker loop. Our structure revealed that the unique residue R54 provides an additional positive charge to the substrate-binding pocket of DrMazF, its mutation significantly affects the endonuclease activity. Thus, our work reports the unique structural and biochemical features of the DrMazE-MazF system.
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Authors: Dhanasingh, I., Lee, S.H.
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Functional and structural characterization of Deinococcus radiodurans R1 MazEF toxin-antitoxin system, Dr0416-Dr0417.,Dhanasingh I, Choi E, Lee J, Lee SH, Hwang J J Microbiol. 2021 Feb;59(2):186-201. doi: 10.1007/s12275-021-0523-z. Epub 2021, Feb 1. PMID:33527318<ref>PMID:33527318</ref>
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Description: Crystal structure of MazE-MazF (Form-III) from Deinococcus radiodurans
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Lee, S.H]]
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<div class="pdbe-citations 7d2n" style="background-color:#fffaf0;"></div>
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[[Category: Dhanasingh, I]]
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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: Deinococcus radiodurans]]
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[[Category: Large Structures]]
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[[Category: Dhanasingh I]]
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[[Category: Lee SH]]

Current revision

Crystal structure of MazE-MazF (Form-III) from Deinococcus radiodurans

PDB ID 7d2n

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