| 001 | 207477 | ||
| 005 | 20250730145808.0 | ||
| 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 |
| 024 | 7 | _ | |a WOS:000346229500007 |2 WOS |
| 024 | 7 | _ | |a pmid:25450593 |2 pmid |
| 024 | 7 | _ | |a openalex:W2047628885 |2 openalex |
| 037 | _ | _ | |a PUBDB-2015-01365 |
| 082 | _ | _ | |a 540 |
| 100 | 1 | _ | |0 P:(DE-H253)PIP1020528 |a Das, Uddipan |b 0 |e Corresponding Author |
| 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 Assemblypetea |
| 260 | _ | _ | |a San Diego, Calif. |b Elsevier |c 2014 |
| 336 | 7 | _ | |0 0 |2 EndNote |a Journal Article |
| 336 | 7 | _ | |2 DRIVER |a article |
| 336 | 7 | _ | |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |a Journal Article |b journal |m journal |s 1445000390_3746 |
| 336 | 7 | _ | |2 BibTeX |a ARTICLE |
| 500 | _ | _ | |3 POF3_Assignment on 2016-02-15 |
| 500 | _ | _ | |3 POF3_Prefill: G:(DE-HGF)POF3-899 |
| 500 | _ | _ | |a (c) Elsevier Inc. Post referee full text in progress. Embargo for full text 1 year from 22. Oct. 2014. |
| 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 (VapB$_2$C$_2$) and two heterotrimers (VapBC$_2$) 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 VapB$_2$C$_2$ and VapBC$_2$ 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. |
| 536 | _ | _ | |0 G:(DE-H253)POF2-P13-20130405 |f POF II |x 0 |c POF2-54G14 |a PETRA Beamline P13 (POF2-54G14) |
| 588 | _ | _ | |a Dataset connected to CrossRef, bib-pubdb1.desy.de |
| 693 | _ | _ | |0 EXP:(DE-H253)P-P13-20150101 |1 EXP:(DE-H253)PETRAIII-20150101 |6 EXP:(DE-H253)P-P13-20150101 |a PETRA III |f PETRA Beamline P13 |x 0 |
| 700 | 1 | _ | |0 P:(DE-H253)PIP1013622 |a Pogenberg, Vivian |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Subhramanyam, Udaya Kumar Tiruttani |b 2 |
| 700 | 1 | _ | |0 P:(DE-H253)PIP1001283 |a Wilmanns, Matthias |b 3 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Gourinath, Samudrala |b 4 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Srinivasan, Alagiri |b 5 |
| 773 | _ | _ | |0 PERI:(DE-600)1469822-5 |a 10.1016/j.jsb.2014.10.002 |g Vol. 188, no. 3, p. 249 - 258 |n 3 |p 249 - 258 |t Journal of structural biology |v 188 |x 1047-8477 |y 2014 |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/207477/files/10.1016_j.jsb.2014.10.002.pdf |y Restricted |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/207477/files/10.1016_j.jsb.2014.10.002.gif?subformat=icon |x icon |y Restricted |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/207477/files/10.1016_j.jsb.2014.10.002.jpg?subformat=icon-1440 |x icon-1440 |y Restricted |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/207477/files/10.1016_j.jsb.2014.10.002.jpg?subformat=icon-180 |x icon-180 |y Restricted |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/207477/files/10.1016_j.jsb.2014.10.002.jpg?subformat=icon-640 |x icon-640 |y Restricted |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/207477/files/10.1016_j.jsb.2014.10.002.jpg?subformat=icon-700 |x icon-700 |y Restricted |
| 856 | 4 | _ | |u https://bib-pubdb1.desy.de/record/207477/files/10.1016_j.jsb.2014.10.002.pdf?subformat=pdfa |x pdfa |y Restricted |
| 909 | C | O | |o oai:bib-pubdb1.desy.de:207477 |p VDB |
| 910 | 1 | _ | |0 I:(DE-HGF)0 |6 P:(DE-H253)PIP1020528 |a Externes Institut |b 0 |k >Extern |
| 910 | 1 | _ | |0 I:(DE-588b)235011-7 |6 P:(DE-H253)PIP1013622 |a Europäisches Laboratorium für Molekularbiologie |b 1 |k EMBL |
| 910 | 1 | _ | |0 I:(DE-HGF)0 |6 P:(DE-H253)PIP1013622 |a Externes Institut |b 1 |k >Extern |
| 910 | 1 | _ | |0 I:(DE-588b)235011-7 |6 P:(DE-H253)PIP1001283 |a Europäisches Laboratorium für Molekularbiologie |b 3 |k EMBL |
| 910 | 1 | _ | |0 I:(DE-HGF)0 |6 P:(DE-H253)PIP1001283 |a Externes Institut |b 3 |k >Extern |
| 913 | 2 | _ | |0 G:(DE-HGF)POF3-622 |1 G:(DE-HGF)POF3-620 |2 G:(DE-HGF)POF3-600 |9 G:(DE-HGF)POF3-6G3 |a DE-HGF |b Forschungsbereich Materie |l Von Materie zu Materialien und Leben |v Facility topic: Research on Matter with Brilliant Light Sources |x 0 |
| 913 | 1 | _ | |0 G:(DE-HGF)POF2-54G14 |1 G:(DE-HGF)POF2-540 |2 G:(DE-HGF)POF2-500 |9 G:(DE-H253)POF2-P13-20130405 |b Struktur der Materie |v PETRA III |x 0 |a DE-H253 |4 G:(DE-HGF)POF |3 G:(DE-HGF)POF2 |l Forschung mit Photonen, Neutronen, Ionen |
| 914 | 1 | _ | |y 2014 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0100 |2 StatID |a JCR |
| 915 | _ | _ | |0 StatID:(DE-HGF)0110 |2 StatID |a WoS |b Science Citation Index |
| 915 | _ | _ | |0 StatID:(DE-HGF)0111 |2 StatID |a WoS |b Science Citation Index Expanded |
| 915 | _ | _ | |0 StatID:(DE-HGF)0150 |2 StatID |a DBCoverage |b Web of Science Core Collection |
| 915 | _ | _ | |0 StatID:(DE-HGF)0199 |2 StatID |a DBCoverage |b Thomson Reuters Master Journal List |
| 915 | _ | _ | |0 StatID:(DE-HGF)0200 |2 StatID |a DBCoverage |b SCOPUS |
| 915 | _ | _ | |0 StatID:(DE-HGF)0300 |2 StatID |a DBCoverage |b Medline |
| 915 | _ | _ | |0 StatID:(DE-HGF)0310 |2 StatID |a DBCoverage |b NCBI Molecular Biology Database |
| 915 | _ | _ | |0 StatID:(DE-HGF)0420 |2 StatID |a Nationallizenz |
| 915 | _ | _ | |0 StatID:(DE-HGF)1030 |2 StatID |a DBCoverage |b Current Contents - Life Sciences |
| 915 | _ | _ | |0 StatID:(DE-HGF)1040 |2 StatID |a DBCoverage |b Zoological Record |
| 915 | _ | _ | |0 StatID:(DE-HGF)1050 |2 StatID |a DBCoverage |b BIOSIS Previews |
| 915 | _ | _ | |0 StatID:(DE-HGF)9900 |2 StatID |a IF < 5 |
| 920 | 1 | _ | |0 I:(DE-H253)EMBL-20120731 |k EMBL |l EMBL |x 0 |
| 980 | _ | _ | |a journal |
| 980 | _ | _ | |a VDB |
| 980 | _ | _ | |a I:(DE-H253)EMBL-20120731 |
| 980 | _ | _ | |a UNRESTRICTED |
| Library | Collection | CLSMajor | CLSMinor | Language | Author |
|---|
guest ::