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| 024 | 7 | _ | |a 10.1016/j.jsb.2014.10.002 |2 doi |
| 024 | 7 | _ | |a 1047-8477 |2 ISSN |
| 024 | 7 | _ | |a 1095-8657 |2 ISSN |
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| 037 | _ | _ | |a FZJ-2014-05967 |
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| 100 | 1 | _ | |a Das, Uddipan |0 P:(DE-HGF)0 |b 0 |
| 245 | _ | _ | |a Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis reveals a two-metal ion dependent PIN-domain ribonuclease and a variable mode of toxin-antitoxin assembly |
| 260 | _ | _ | |a San Diego, Calif. |c 2014 |b Elsevier |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1420462993_23887 |2 PUB:(DE-HGF) |
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| 336 | 7 | _ | |a article |2 DRIVER |
| 500 | _ | _ | |a Article in press |
| 520 | _ | _ | |a Although PIN (PilT N-terminal)-domain proteins are known to have ribonuclease activity, their specific mechanism of action remains unknown. VapCs form a family of ribonucleases that possess a PIN-domain assembly and are known as toxins. The activities of VapCs are impaired by VapB antitoxins. Here we present the crystal structure of the VapBC-15 toxin–antitoxin complex from Mycobacterium tuberculosis determined to 2.1 Å resolution. The VapB-15 and VapC-15 components assemble into one heterotetramer (VapB2C2) and two heterotrimers (VapBC2) in each asymmetric unit of the crystal. The active site of VapC-15 toxin consists of a cluster of acidic amino acid residues and two divalent metal ions, forming a well organised ribonuclease active site. The distribution of the catalytic-site residues of the VapC-15 toxin is similar to that of T4 RNase H and of Methanococcus jannaschii FEN-1, providing strong evidence that these three proteins share a similar mechanism of activity. The presence of both VapB2C2 and VapBC2 emphasizes the fact that the same antitoxin can bind the toxin in 1:1 and 1:2 ratios. The crystal structure determination of the VapBC-15 complex reveals for the first time a PIN-domain ribonuclease protein that shows two metal ions at the active site and a variable mode of toxin–antitoxin assembly. The structure further shows that VapB-15 antitoxin binds to the same groove meant for the binding of putative substrate (RNA), resulting in the inhibition of VapC-15’s toxicity. |
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| 700 | 1 | _ | |a Pogenberg, Vivian |0 P:(DE-HGF)0 |b 1 |
| 700 | 1 | _ | |a Tiruttani Subhramanyam, Udaya Kumar |0 P:(DE-Juel1)131986 |b 2 |u fzj |
| 700 | 1 | _ | |a Matthias, Wilmanns |0 P:(DE-HGF)0 |b 3 |
| 700 | 1 | _ | |a Gourinath, Samudrala |0 P:(DE-HGF)0 |b 4 |
| 700 | 1 | _ | |a Srinivana, Alagiri |0 P:(DE-HGF)0 |b 5 |e Corresponding Author |
| 773 | _ | _ | |a 10.1016/j.jsb.2014.10.002 |g p. S1047847714002111 |0 PERI:(DE-600)1469822-5 |n 3 |p 249–258 |t Journal of structural biology |v 188 |y 2014 |x 1047-8477 |
| 856 | 4 | _ | |u http://www.sciencedirect.com/science/article/pii/S1047847714002111# |
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