000016637 001__ 16637
000016637 005__ 20200402205754.0
000016637 0247_ $$2pmid$$apmid:21543878
000016637 0247_ $$2pmc$$apmc:PMC3087657
000016637 0247_ $$2DOI$$a10.1107/S1744309111010876
000016637 0247_ $$2WOS$$aWOS:000290235900025
000016637 037__ $$aPreJuSER-16637
000016637 041__ $$aeng
000016637 082__ $$a530
000016637 084__ $$2WoS$$aBiochemical Research Methods
000016637 084__ $$2WoS$$aBiochemistry & Molecular Biology
000016637 084__ $$2WoS$$aBiophysics
000016637 084__ $$2WoS$$aCrystallography
000016637 1001_ $$0P:(DE-HGF)0$$aSchwarz, C.K.W.$$b0
000016637 245__ $$aCrystallisation and preliminary X-ray crystallographic studies of an oligomeric species of a refolded C39 peptidase-like domain of the Escherichia coli ABC transporter Haemolysin B
000016637 260__ $$aOxford [u.a.]$$bBlackwell$$c2011
000016637 300__ $$a630 - 633
000016637 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
000016637 3367_ $$2DataCite$$aOutput Types/Journal article
000016637 3367_ $$00$$2EndNote$$aJournal Article
000016637 3367_ $$2BibTeX$$aARTICLE
000016637 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000016637 3367_ $$2DRIVER$$aarticle
000016637 440_0 $$013801$$aActa Crystallographica Section F-Structural Biology and Crystallization Communications$$v67$$x1744-3091$$y5
000016637 500__ $$3POF3_Assignment on 2016-02-29
000016637 500__ $$aWe would like to acknowledge Solvej Siedler for important assistance during the initial stages of this project. This work was funded by the EDICT (European Initiative on Channels and Transporters) consortium FP7 Theme (Health-2007-2.1.1-5) to BT and LS. We thank the Ministry of Innovation, Science and Research of the German Federal State North Rhine-Westphalia (NRW) and the Heinrich Heine University Dusseldorf (scholarship from the CLIB-Graduate Cluster Industrial Biotechnology to CKWS).
000016637 520__ $$aThe ABC transporter haemolysin B (HlyB) from Escherichia coli is part of a type I secretion system that translocates a 110 kDa toxin in one step across both membranes of this Gram-negative bacterium in an ATP-dependent manner. Sequence analysis indicates that HlyB contains a C39 peptidase-like domain at its N-terminus. C39 domains are thiol-dependent peptidases that cleave their substrates after a GG motif. Interestingly, the catalytically invariant cysteine is replaced by a tyrosine in the C39-like domain of HlyB. Here, the overexpression, purification and crystallization of the isolated C39-like domain are described as a first step towards obtaining structural insights into this domain and eventually answering the question concerning the function of a degenerated C39 domain in the ABC transporter HlyB.
000016637 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000016637 536__ $$0G:(DE-Juel1)FUEK505$$2G:(DE-HGF)$$aBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$cP45$$x1
000016637 588__ $$aDataset connected to Web of Science, Pubmed
000016637 650_2 $$2MeSH$$aATP-Binding Cassette Transporters: chemistry
000016637 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000016637 650_2 $$2MeSH$$aCarrier Proteins: chemistry
000016637 650_2 $$2MeSH$$aCrystallization
000016637 650_2 $$2MeSH$$aCrystallography, X-Ray
000016637 650_2 $$2MeSH$$aEscherichia coli: chemistry
000016637 650_2 $$2MeSH$$aHemolysin Proteins: chemistry
000016637 650_2 $$2MeSH$$aProtein Multimerization
000016637 650_2 $$2MeSH$$aProtein Refolding
000016637 650_7 $$00$$2NLM Chemicals$$aATP-Binding Cassette Transporters
000016637 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000016637 650_7 $$00$$2NLM Chemicals$$aCarrier Proteins
000016637 650_7 $$00$$2NLM Chemicals$$aHemolysin Proteins
000016637 650_7 $$00$$2NLM Chemicals$$aHlyb protein, Bacteria
000016637 650_7 $$2WoSType$$aJ
000016637 7001_ $$0P:(DE-HGF)0$$aTschapek, B.$$b1
000016637 7001_ $$0P:(DE-HGF)0$$aJumpertz, T.$$b2
000016637 7001_ $$0P:(DE-HGF)0$$aJenewein, S.$$b3
000016637 7001_ $$0P:(DE-Juel1)VDB94799$$aLecher, J.$$b4$$uFZJ
000016637 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b5$$uFZJ
000016637 7001_ $$0P:(DE-HGF)0$$aPanjikar, S.$$b6
000016637 7001_ $$0P:(DE-HGF)0$$aHalland, B.$$b7
000016637 7001_ $$0P:(DE-HGF)0$$aSmits, S.H.J.$$b8
000016637 7001_ $$0P:(DE-HGF)0$$aSchmitt, L.$$b9
000016637 773__ $$0PERI:(DE-600)2175956-X$$a10.1107/S1744309111010876$$gVol. 67, p. 630 - 633$$p630 - 633$$q67<630 - 633$$tActa crystallographica / F$$v67$$x1744-3091$$y2011
000016637 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3087657
000016637 909CO $$ooai:juser.fz-juelich.de:16637$$pVDB
000016637 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000016637 9141_ $$y2011
000016637 9131_ $$0G:(DE-Juel1)FUEK409$$aDE-HGF$$bGesundheit$$kP33$$lFunktion und Dysfunktion des Nervensystems$$vFunktion und Dysfunktion des Nervensystems$$x0
000016637 9131_ $$0G:(DE-Juel1)FUEK505$$aDE-HGF$$bSchlüsseltechnologien$$kP45$$lBiologische Informationsverarbeitung$$vBioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung$$x1
000016637 9132_ $$0G:(DE-HGF)POF3-559H$$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$$vAddenda$$x0
000016637 9201_ $$0I:(DE-Juel1)ICS-6-20110106$$gICS$$kICS-6$$lStrukturbiochemie$$x0
000016637 970__ $$aVDB:(DE-Juel1)130808
000016637 980__ $$aVDB
000016637 980__ $$aConvertedRecord
000016637 980__ $$ajournal
000016637 980__ $$aI:(DE-Juel1)ICS-6-20110106
000016637 980__ $$aUNRESTRICTED
000016637 981__ $$aI:(DE-Juel1)IBI-7-20200312