| 001 | 16637 | ||
| 005 | 20200402205754.0 | ||
| 024 | 7 | _ | |2 pmid |a pmid:21543878 |
| 024 | 7 | _ | |2 pmc |a pmc:PMC3087657 |
| 024 | 7 | _ | |2 DOI |a 10.1107/S1744309111010876 |
| 024 | 7 | _ | |2 WOS |a WOS:000290235900025 |
| 037 | _ | _ | |a PreJuSER-16637 |
| 041 | _ | _ | |a eng |
| 082 | _ | _ | |a 530 |
| 084 | _ | _ | |2 WoS |a Biochemical Research Methods |
| 084 | _ | _ | |2 WoS |a Biochemistry & Molecular Biology |
| 084 | _ | _ | |2 WoS |a Biophysics |
| 084 | _ | _ | |2 WoS |a Crystallography |
| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Schwarz, C.K.W. |b 0 |
| 245 | _ | _ | |a Crystallisation 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 |
| 260 | _ | _ | |a Oxford [u.a.] |b Blackwell |c 2011 |
| 300 | _ | _ | |a 630 - 633 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |
| 336 | 7 | _ | |a Output Types/Journal article |2 DataCite |
| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 336 | 7 | _ | |a JOURNAL_ARTICLE |2 ORCID |
| 336 | 7 | _ | |a article |2 DRIVER |
| 440 | _ | 0 | |0 13801 |a Acta Crystallographica Section F-Structural Biology and Crystallization Communications |v 67 |x 1744-3091 |y 5 |
| 500 | _ | _ | |3 POF3_Assignment on 2016-02-29 |
| 500 | _ | _ | |a We 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). |
| 520 | _ | _ | |a The 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. |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK409 |2 G:(DE-HGF) |a Funktion und Dysfunktion des Nervensystems |c P33 |x 0 |
| 536 | _ | _ | |0 G:(DE-Juel1)FUEK505 |2 G:(DE-HGF) |a BioSoft: Makromolekulare Systeme und biologische Informationsverarbeitung |c P45 |x 1 |
| 588 | _ | _ | |a Dataset connected to Web of Science, Pubmed |
| 650 | _ | 2 | |2 MeSH |a ATP-Binding Cassette Transporters: chemistry |
| 650 | _ | 2 | |2 MeSH |a Bacterial Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Carrier Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Crystallization |
| 650 | _ | 2 | |2 MeSH |a Crystallography, X-Ray |
| 650 | _ | 2 | |2 MeSH |a Escherichia coli: chemistry |
| 650 | _ | 2 | |2 MeSH |a Hemolysin Proteins: chemistry |
| 650 | _ | 2 | |2 MeSH |a Protein Multimerization |
| 650 | _ | 2 | |2 MeSH |a Protein Refolding |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a ATP-Binding Cassette Transporters |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Bacterial Proteins |
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| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Hemolysin Proteins |
| 650 | _ | 7 | |0 0 |2 NLM Chemicals |a Hlyb protein, Bacteria |
| 650 | _ | 7 | |2 WoSType |a J |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Tschapek, B. |b 1 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Jumpertz, T. |b 2 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Jenewein, S. |b 3 |
| 700 | 1 | _ | |0 P:(DE-Juel1)VDB94799 |a Lecher, J. |b 4 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-Juel1)132029 |a Willbold, D. |b 5 |u FZJ |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Panjikar, S. |b 6 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Halland, B. |b 7 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Smits, S.H.J. |b 8 |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Schmitt, L. |b 9 |
| 773 | _ | _ | |0 PERI:(DE-600)2175956-X |a 10.1107/S1744309111010876 |g Vol. 67, p. 630 - 633 |p 630 - 633 |q 67<630 - 633 |t Acta crystallographica / F |v 67 |x 1744-3091 |y 2011 |
| 856 | 7 | _ | |2 Pubmed Central |u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3087657 |
| 909 | C | O | |o oai:juser.fz-juelich.de:16637 |p VDB |
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| 913 | 2 | _ | |a DE-HGF |b Key Technologies |l BioSoft – Fundamentals for future Technologies in the fields of Soft Matter and Life Sciences |1 G:(DE-HGF)POF3-550 |0 G:(DE-HGF)POF3-559H |2 G:(DE-HGF)POF3-500 |v Addenda |x 0 |
| 914 | 1 | _ | |y 2011 |
| 915 | _ | _ | |0 StatID:(DE-HGF)0010 |a JCR/ISI refereed |
| 920 | 1 | _ | |0 I:(DE-Juel1)ICS-6-20110106 |g ICS |k ICS-6 |l Strukturbiochemie |x 0 |
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| 980 | _ | _ | |a UNRESTRICTED |
| 981 | _ | _ | |a I:(DE-Juel1)IBI-7-20200312 |
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