3dbo

<table><tr><td colspan='2'>[[3dbo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DBO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DBO FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv0626, MT0654 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU]), Rv0627 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>

[[https://www.uniprot.org/uniprot/VAPB5_MYCTO VAPB5_MYCTO]] Probable antitoxin component of a probable toxin-antitoxin (TA) module. The cognate toxin is VapC5 (By similarity). [[https://www.uniprot.org/uniprot/VAPC5_MYCTU VAPC5_MYCTU]] Probable toxic component of a type II toxin-antitoxin (TA) module. The cognate antitoxin is VapB5. Has limited RNase activity on substrates; activity is seen with a VapC5-VapB5 complex.<ref>PMID:18952600</ref>

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== Publication Abstract from PubMed ==

In prokaryotes, cognate toxin-antitoxin pairs have long been known, but no three-dimensional structure has been available for any given complex from Mycobacterium tuberculosis. Here we report the crystal structure and activity of a member of the VapBC family of complexes from M. tuberculosis. The toxin VapC-5 is a compact, 150 residues, two domain alpha/beta protein. Bent around the toxin is the VapB-5 antitoxin, a 33-residue alpha-helix. Assays suggest that the toxin is an Mg-enabled endoribonuclease, inhibited by the antitoxin. The lack of DNase activity is consistent with earlier suggestions that the complex represses its own operon. Furthermore, analysis of the interactions in the binding of the antitoxin to the toxin suggest that exquisite control is required to protect the bacteria cell from toxic VapC-5.

Structure and proposed activity of a member of the VapBC family of toxin-antitoxin systems. VapBC-5 from Mycobacterium tuberculosis.,Miallau L, Faller M, Chiang J, Arbing M, Guo F, Cascio D, Eisenberg D J Biol Chem. 2009 Jan 2;284(1):276-83. Epub 2008 Oct 24. PMID:18952600<ref>PMID:18952600</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3dbo" style="background-color:#fffaf0;"></div>

[[Category: Myctu]]

[[Category: Cascio, D]]

[[Category: Eisenberg, D]]

[[Category: ISFI, Integrated Center for Structure and Function Innovation]]

[[Category: Miallau, L]]

[[Category: Vapbc]]