000172498 001__ 172498
000172498 005__ 20210129214438.0
000172498 0247_ $$2doi$$a10.1016/j.jsb.2014.10.002
000172498 0247_ $$2ISSN$$a1047-8477
000172498 0247_ $$2ISSN$$a1095-8657
000172498 0247_ $$2WOS$$aWOS:000346229500007
000172498 037__ $$aFZJ-2014-05967
000172498 082__ $$a540
000172498 1001_ $$0P:(DE-HGF)0$$aDas, Uddipan$$b0
000172498 245__ $$aCrystal 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
000172498 260__ $$aSan Diego, Calif.$$bElsevier$$c2014
000172498 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1420462993_23887
000172498 3367_ $$2DataCite$$aOutput Types/Journal article
000172498 3367_ $$00$$2EndNote$$aJournal Article
000172498 3367_ $$2BibTeX$$aARTICLE
000172498 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000172498 3367_ $$2DRIVER$$aarticle
000172498 500__ $$aArticle in press
000172498 520__ $$aAlthough 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.
000172498 536__ $$0G:(DE-HGF)POF2-452$$a452 - Structural Biology (POF2-452)$$cPOF2-452$$fPOF II$$x0
000172498 588__ $$aDataset connected to CrossRef, juser.fz-juelich.de
000172498 7001_ $$0P:(DE-HGF)0$$aPogenberg, Vivian$$b1
000172498 7001_ $$0P:(DE-Juel1)131986$$aTiruttani Subhramanyam, Udaya Kumar$$b2$$ufzj
000172498 7001_ $$0P:(DE-HGF)0$$aMatthias, Wilmanns$$b3
000172498 7001_ $$0P:(DE-HGF)0$$aGourinath, Samudrala$$b4
000172498 7001_ $$0P:(DE-HGF)0$$aSrinivana, Alagiri$$b5$$eCorresponding Author
000172498 773__ $$0PERI:(DE-600)1469822-5$$a10.1016/j.jsb.2014.10.002$$gp. S1047847714002111$$n3$$p249–258$$tJournal of structural biology$$v188$$x1047-8477$$y2014
000172498 8564_ $$uhttp://www.sciencedirect.com/science/article/pii/S1047847714002111#
000172498 8564_ $$uhttps://juser.fz-juelich.de/record/172498/files/FZJ-2014-05967.pdf$$yRestricted
000172498 909CO $$ooai:juser.fz-juelich.de:172498$$pVDB
000172498 9101_ $$0I:(DE-588b)5008462-8$$6P:(DE-Juel1)131986$$aForschungszentrum Jülich GmbH$$b2$$kFZJ
000172498 9132_ $$0G:(DE-HGF)POF3-551$$1G:(DE-HGF)POF3-550$$2G:(DE-HGF)POF3-500$$aDE-HGF$$bKey Technologies$$lBioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences$$vFunctional Macromolecules and Complexes$$x0
000172498 9131_ $$0G:(DE-HGF)POF2-452$$1G:(DE-HGF)POF2-450$$2G:(DE-HGF)POF2-400$$3G:(DE-HGF)POF2$$4G:(DE-HGF)POF$$aDE-HGF$$bSchlüsseltechnologien$$lBioSoft$$vStructural Biology$$x0
000172498 9141_ $$y2014
000172498 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR
000172498 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000172498 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000172498 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000172498 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bThomson Reuters Master Journal List
000172498 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000172498 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000172498 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000172498 915__ $$0StatID:(DE-HGF)0420$$2StatID$$aNationallizenz
000172498 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000172498 915__ $$0StatID:(DE-HGF)1040$$2StatID$$aDBCoverage$$bZoological Record
000172498 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000172498 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF <  5
000172498 920__ $$lyes
000172498 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$kICS-6$$lStrukturbiochemie $$x0
000172498 980__ $$ajournal
000172498 980__ $$aVDB
000172498 980__ $$aI:(DE-Juel1)ICS-6-20110106
000172498 980__ $$aUNRESTRICTED
000172498 981__ $$aI:(DE-Juel1)IBI-7-20200312