000417860 001__ 417860
000417860 005__ 20250729165439.0
000417860 0247_ $$2doi$$a10.1016/j.jmb.2017.11.016
000417860 0247_ $$2ISSN$$a0022-2836
000417860 0247_ $$2ISSN$$a1089-8638
000417860 0247_ $$2datacite_doi$$a10.3204/PUBDB-2019-00036
000417860 0247_ $$2pmid$$apmid:29258816
000417860 0247_ $$2WOS$$aWOS:000429398200006
000417860 0247_ $$2openalex$$aopenalex:W2775220904
000417860 037__ $$aPUBDB-2019-00036
000417860 041__ $$aEnglish
000417860 082__ $$a610
000417860 1001_ $$aPiasecka, Anna$$b0
000417860 245__ $$aThe Y. bercovieri Anbu crystal structure sheds light on the evolution of highly (pseudo)symmetric multimers
000417860 260__ $$aAmsterdam [u.a.]$$bElsevier$$c2018
000417860 3367_ $$2DRIVER$$aarticle
000417860 3367_ $$2DataCite$$aOutput Types/Journal article
000417860 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1546952235_19755
000417860 3367_ $$2BibTeX$$aARTICLE
000417860 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000417860 3367_ $$00$$2EndNote$$aJournal Article
000417860 520__ $$aAncestral β-subunit (Anbu) is homologous to HslV and 20S proteasomes. Based on its phylogenetic distribution and sequence clustering, Anbu has been proposed as the “ancestral” form of proteasomes. Here, we report biochemical data, small-angle X-ray scattering results, negative-stain electron microscopy micrographs and a crystal structure of the Anbu particle from Yersinia bercovieri (YbAnbu). All data are consistent with YbAnbu forming defined 12–14 subunit multimers that differ in shape from both HslV and 20S proteasomes. The crystal structure reveals that YbAnbu subunits form tight dimers, held together in part by the Anbu specific C-terminal helices. These dimers (“protomers”) further assemble into a low-rise left-handed staircase. The lock-washer shape of YbAnbu is consistent with the presence of defined multimers, X-ray diffraction data in solution and negative-stain electron microscopy images. The presented structure suggests a possible evolutionary pathway from helical filaments to highly symmetric or pseudosymmetric multimer structures. YbAnbu subunits have the Ntn-hydrolase fold, a putative S1 pocket and conserved candidate catalytic residues Thr1, Asp17 and Lys32(33). Nevertheless, we did not detect any YbAnbu peptidase or amidase activity. However, we could document orthophosphate production from ATP catalyzed by the ATP-grasp protein encoded in the Y. bercovieri Anbu operon. 
000417860 536__ $$0G:(DE-HGF)POF3-899$$a899 - ohne Topic (POF3-899)$$cPOF3-899$$fPOF III$$x0
000417860 588__ $$aDataset connected to CrossRef
000417860 693__ $$0EXP:(DE-H253)D-D1.2-20150101$$1EXP:(DE-H253)DORISIII-20150101$$6EXP:(DE-H253)D-D1.2-20150101$$aDORIS III$$fDORIS Beamline D1.2$$x0
000417860 7001_ $$0P:(DE-H253)PIP1011581$$aCzapinska, Honorata$$b1
000417860 7001_ $$aVielberg, Marie-Theres$$b2
000417860 7001_ $$aSzczepanowski, Roman H.$$b3
000417860 7001_ $$aKiefersauer, Reiner$$b4
000417860 7001_ $$aReed, Simon$$b5
000417860 7001_ $$aGroll, Michael$$b6
000417860 7001_ $$0P:(DE-HGF)0$$aBochtler, Matthias$$b7$$eCorresponding author
000417860 773__ $$0PERI:(DE-600)1355192-9$$a10.1016/j.jmb.2017.11.016$$gVol. 430, no. 5, p. 611 - 627$$n5$$p611 - 627$$tJournal of molecular biology$$v430$$x0022-2836$$y2018
000417860 8564_ $$uhttps://bib-pubdb1.desy.de/record/417860/files/1-s2.0-S0022283617305909-main.pdf$$yOpenAccess
000417860 8564_ $$uhttps://bib-pubdb1.desy.de/record/417860/files/1-s2.0-S0022283617305909-main.gif?subformat=icon$$xicon$$yOpenAccess
000417860 8564_ $$uhttps://bib-pubdb1.desy.de/record/417860/files/1-s2.0-S0022283617305909-main.jpg?subformat=icon-1440$$xicon-1440$$yOpenAccess
000417860 8564_ $$uhttps://bib-pubdb1.desy.de/record/417860/files/1-s2.0-S0022283617305909-main.jpg?subformat=icon-180$$xicon-180$$yOpenAccess
000417860 8564_ $$uhttps://bib-pubdb1.desy.de/record/417860/files/1-s2.0-S0022283617305909-main.jpg?subformat=icon-640$$xicon-640$$yOpenAccess
000417860 8564_ $$uhttps://bib-pubdb1.desy.de/record/417860/files/1-s2.0-S0022283617305909-main.pdf?subformat=pdfa$$xpdfa$$yOpenAccess
000417860 909CO $$ooai:bib-pubdb1.desy.de:417860$$pdnbdelivery$$pdriver$$pVDB$$popen_access$$popenaire
000417860 9101_ $$0I:(DE-HGF)0$$6P:(DE-H253)PIP1011581$$aExternes Institut$$b1$$kExtern
000417860 9131_ $$0G:(DE-HGF)POF3-899$$1G:(DE-HGF)POF3-890$$2G:(DE-HGF)POF3-800$$3G:(DE-HGF)POF3$$4G:(DE-HGF)POF$$aDE-HGF$$bProgrammungebundene Forschung$$lohne Programm$$vohne Topic$$x0
000417860 9141_ $$y2018
000417860 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS
000417860 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences
000417860 915__ $$0LIC:(DE-HGF)CCBY4$$2HGFVOC$$aCreative Commons Attribution CC BY 4.0
000417860 915__ $$0StatID:(DE-HGF)0600$$2StatID$$aDBCoverage$$bEbsco Academic Search
000417860 915__ $$0StatID:(DE-HGF)0100$$2StatID$$aJCR$$bJ MOL BIOL : 2017
000417860 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection
000417860 915__ $$0StatID:(DE-HGF)0110$$2StatID$$aWoS$$bScience Citation Index
000417860 915__ $$0StatID:(DE-HGF)0111$$2StatID$$aWoS$$bScience Citation Index Expanded
000417860 915__ $$0StatID:(DE-HGF)9900$$2StatID$$aIF < 5
000417860 915__ $$0StatID:(DE-HGF)0510$$2StatID$$aOpenAccess
000417860 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer Review$$bASC
000417860 915__ $$0StatID:(DE-HGF)0310$$2StatID$$aDBCoverage$$bNCBI Molecular Biology Database
000417860 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews
000417860 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline
000417860 915__ $$0StatID:(DE-HGF)0420$$2StatID$$aNationallizenz
000417860 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bClarivate Analytics Master Journal List
000417860 9201_ $$0I:(DE-H253)EMBL-User-20120814$$kEMBL-User$$lEMBL-User$$x0
000417860 980__ $$ajournal
000417860 980__ $$aVDB
000417860 980__ $$aUNRESTRICTED
000417860 980__ $$aI:(DE-H253)EMBL-User-20120814
000417860 9801_ $$aFullTexts