Home > Workflow collections > Publication Charges > A combination of mutational and computational scanning guides the design of an artificial ligand-binding controlled lipase > print

001     829442
005     20240619091845.0
024 7 _ |a 10.1038/srep42592
|2 doi
024 7 _ |a 2128/14207
|2 Handle
024 7 _ |a WOS:000394417100001
|2 WOS
037 _ _ |a FZJ-2017-03146
041 _ _ |a English
082 _ _ |a 000
100 1 _ |a Kaschner, Marco
|0 P:(DE-Juel1)131462
|b 0
245 _ _ |a A combination of mutational and computational scanning guides the design of an artificial ligand-binding controlled lipase
260 _ _ |a London
|c 2017
|b Nature Publishing Group
336 7 _ |a article
|2 DRIVER
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|b journal
|m journal
|0 PUB:(DE-HGF)16
|s 1516200041_24901
|2 PUB:(DE-HGF)
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a Journal Article
|0 0
|2 EndNote
520 _ _ |a Allostery, i.e. the control of enzyme activity by a small molecule at a location distant from the enzyme’s active site, represents a mechanism essential for sustaining life. The rational design of allostery is a non-trivial task but can be achieved by fusion of a sensory domain, which responds to environmental stimuli with a change in its structure. Hereby, the site of domain fusion is difficult to predict. We here explore the possibility to rationally engineer allostery into the naturally not allosterically regulated Bacillus subtilis lipase A, by fusion of the citrate-binding sensor-domain of the CitA sensory-kinase of Klebsiella pneumoniae. The site of domain fusion was rationally determined based on whole-protein site-saturation mutagenesis data, complemented by computational evolutionary-coupling analyses. Functional assays, combined with biochemical and biophysical studies suggest a mechanism for control, similar but distinct to the one of the parent CitA protein, with citrate acting as an indirect modulator of Triton-X100 inhibition of the fusion protein. Our study demonstrates that the introduction of ligand-dependent regulatory control by domain fusion is surprisingly facile, suggesting that the catalytic mechanism of some enzymes may be evolutionary optimized in a way that it can easily be perturbed by small conformational changes.
536 _ _ |a 551 - Functional Macromolecules and Complexes (POF3-551)
|0 G:(DE-HGF)POF3-551
|c POF3-551
|f POF III
|x 0
536 _ _ |a 6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
|0 G:(DE-HGF)POF3-6G4
|c POF3-623
|f POF III
|x 1
536 _ _ |a 6215 - Soft Matter, Health and Life Sciences (POF3-621)
|0 G:(DE-HGF)POF3-6215
|c POF3-621
|f POF III
|x 2
536 _ _ |a 581 - Biotechnology (POF3-581)
|0 G:(DE-HGF)POF3-581
|c POF3-581
|f POF III
|x 3
588 _ _ |a Dataset connected to CrossRef
700 1 _ |a Schillinger, Oliver
|0 P:(DE-Juel1)157850
|b 1
700 1 _ |a Fettweiss, Timo
|0 P:(DE-Juel1)162158
|b 2
700 1 _ |a Nutschel, Christina
|0 P:(DE-HGF)0
|b 3
700 1 _ |a Krause, Frank
|0 P:(DE-HGF)0
|b 4
700 1 _ |a Fulton, Alexander
|0 P:(DE-Juel1)143642
|b 5
700 1 _ |a Strodel, Birgit
|0 P:(DE-Juel1)132024
|b 6
700 1 _ |a Stadler, Andreas
|0 P:(DE-Juel1)140278
|b 7
700 1 _ |a Jaeger, Karl-Erich
|0 P:(DE-Juel1)131457
|b 8
700 1 _ |a Krauss, Ulrich
|0 P:(DE-Juel1)131482
|b 9
|e Corresponding author
773 _ _ |a 10.1038/srep42592
|g Vol. 7, p. 42592 -
|0 PERI:(DE-600)2615211-3
|p 42592 -
|t Scientific reports
|v 7
|y 2017
|x 2045-2322
856 4 _ |u https://juser.fz-juelich.de/record/829442/files/srep42592.pdf
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/829442/files/srep42592.gif?subformat=icon
|x icon
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/829442/files/srep42592.jpg?subformat=icon-1440
|x icon-1440
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/829442/files/srep42592.jpg?subformat=icon-180
|x icon-180
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/829442/files/srep42592.jpg?subformat=icon-640
|x icon-640
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/829442/files/srep42592.pdf?subformat=pdfa
|x pdfa
|y OpenAccess
909 C O |o oai:juser.fz-juelich.de:829442
|p openaire
|p open_access
|p OpenAPC
|p driver
|p VDB
|p openCost
|p dnbdelivery
910 1 _ |a Forschungszentrum Jülich
|0 I:(DE-588b)5008462-8
|k FZJ
|b 1
|6 P:(DE-Juel1)157850
910 1 _ |a Forschungszentrum Jülich
|0 I:(DE-588b)5008462-8
|k FZJ
|b 2
|6 P:(DE-Juel1)162158
910 1 _ |a Forschungszentrum Jülich
|0 I:(DE-588b)5008462-8
|k FZJ
|b 6
|6 P:(DE-Juel1)132024
910 1 _ |a Forschungszentrum Jülich
|0 I:(DE-588b)5008462-8
|k FZJ
|b 7
|6 P:(DE-Juel1)140278
910 1 _ |a Forschungszentrum Jülich
|0 I:(DE-588b)5008462-8
|k FZJ
|b 8
|6 P:(DE-Juel1)131457
910 1 _ |a Forschungszentrum Jülich
|0 I:(DE-588b)5008462-8
|k FZJ
|b 9
|6 P:(DE-Juel1)131482
913 1 _ |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)POF3-551
|2 G:(DE-HGF)POF3-500
|v Functional Macromolecules and Complexes
|x 0
|4 G:(DE-HGF)POF
|3 G:(DE-HGF)POF3
913 1 _ |a DE-HGF
|b Forschungsbereich Materie
|l Von Materie zu Materialien und Leben
|1 G:(DE-HGF)POF3-620
|0 G:(DE-HGF)POF3-623
|2 G:(DE-HGF)POF3-600
|v Facility topic: Neutrons for Research on Condensed Matter
|9 G:(DE-HGF)POF3-6G4
|x 1
|4 G:(DE-HGF)POF
|3 G:(DE-HGF)POF3
913 1 _ |a DE-HGF
|b Forschungsbereich Materie
|l Von Materie zu Materialien und Leben
|1 G:(DE-HGF)POF3-620
|0 G:(DE-HGF)POF3-621
|2 G:(DE-HGF)POF3-600
|v In-house research on the structure, dynamics and function of matter
|9 G:(DE-HGF)POF3-6215
|x 2
|4 G:(DE-HGF)POF
|3 G:(DE-HGF)POF3
913 1 _ |a DE-HGF
|b Key Technologies
|l Key Technologies for the Bioeconomy
|1 G:(DE-HGF)POF3-580
|0 G:(DE-HGF)POF3-581
|2 G:(DE-HGF)POF3-500
|v Biotechnology
|x 3
|4 G:(DE-HGF)POF
|3 G:(DE-HGF)POF3
914 1 _ |y 2017
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0200
|2 StatID
|b SCOPUS
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1050
|2 StatID
|b BIOSIS Previews
915 _ _ |a Creative Commons Attribution CC BY 4.0
|0 LIC:(DE-HGF)CCBY4
|2 HGFVOC
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1040
|2 StatID
|b Zoological Record
915 _ _ |a JCR
|0 StatID:(DE-HGF)0100
|2 StatID
|b SCI REP-UK : 2015
915 _ _ |a IF >= 5
|0 StatID:(DE-HGF)9905
|2 StatID
|b SCI REP-UK : 2015
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0501
|2 StatID
|b DOAJ Seal
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0500
|2 StatID
|b DOAJ
915 _ _ |a WoS
|0 StatID:(DE-HGF)0110
|2 StatID
|b Science Citation Index
915 _ _ |a WoS
|0 StatID:(DE-HGF)0111
|2 StatID
|b Science Citation Index Expanded
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0150
|2 StatID
|b Web of Science Core Collection
915 _ _ |a OpenAccess
|0 StatID:(DE-HGF)0510
|2 StatID
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1150
|2 StatID
|b Current Contents - Physical, Chemical and Earth Sciences
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0310
|2 StatID
|b NCBI Molecular Biology Database
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0300
|2 StatID
|b Medline
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0199
|2 StatID
|b Thomson Reuters Master Journal List
920 1 _ |0 I:(DE-Juel1)ICS-1-20110106
|k ICS-1
|l Neutronenstreuung
|x 0
920 1 _ |0 I:(DE-Juel1)JCNS-1-20110106
|k Neutronenstreuung ; JCNS-1
|l Neutronenstreuung
|x 1
920 1 _ |0 I:(DE-Juel1)ICS-6-20110106
|k ICS-6
|l Strukturbiochemie
|x 2
920 1 _ |0 I:(DE-Juel1)IMET-20090612
|k IMET
|l Institut für Molekulare Enzymtechnologie (HHUD)
|x 3
980 1 _ |a APC
980 1 _ |a FullTexts
980 _ _ |a journal
980 _ _ |a VDB
980 _ _ |a I:(DE-Juel1)ICS-1-20110106
980 _ _ |a I:(DE-Juel1)JCNS-1-20110106
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
980 _ _ |a I:(DE-Juel1)IMET-20090612
980 _ _ |a APC
980 _ _ |a UNRESTRICTED
981 _ _ |a I:(DE-Juel1)IBI-8-20200312
981 _ _ |a I:(DE-Juel1)JCNS-1-20110106
981 _ _ |a I:(DE-Juel1)IBI-7-20200312

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21