Home > Workflow collections > Publication Charges > On the potential alternate binding change mechanism in a dimeric structure of Pyruvate Phosphate Dikinase > print

001     837023
005     20220930130130.0
024 7 _ |a 10.1038/s41598-017-08521-w
|2 doi
024 7 _ |a 2128/15158
|2 Handle
024 7 _ |a WOS:000407559100020
|2 WOS
037 _ _ |a FZJ-2017-06039
041 _ _ |a English
082 _ _ |a 000
100 1 _ |a Ciupka, Daniel
|0 P:(DE-HGF)0
|b 0
245 _ _ |a On the potential alternate binding change mechanism in a dimeric structure of Pyruvate Phosphate Dikinase
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 1504179501_31194
|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 The pyruvate phosphate dikinase (PPDK) reaction mechanism is characterized by a distinct spatial separation of reaction centers and large conformational changes involving an opening-closing motion of the nucleotide-binding domain (NBD) and a swiveling motion of the central domain (CD). However, why PPDK is active only in a dimeric form and to what extent an alternate binding change mechanism could underlie this fact has remained elusive. We performed unbiased molecular dynamics simulations, configurational free energy computations, and rigidity analysis to address this question. Our results support the hypothesis that PPDK dimerization influences the opening-closing motion of the NBDs, and that this influence is mediated via the CDs of both chains. Such an influence would be a prerequisite for an alternate binding change mechanism to occur. To the best of our knowledge, this is the first time that a possible explanation has been suggested as to why only dimeric PPDK is active.
536 _ _ |a 511 - Computational Science and Mathematical Methods (POF3-511)
|0 G:(DE-HGF)POF3-511
|c POF3-511
|f POF III
|x 0
536 _ _ |a Investigating the swiveling domain mechanism of the Pyruvate phosphate dikinase (PPDK) (hdd14_20140501)
|0 G:(DE-Juel1)hdd14_20140501
|c hdd14_20140501
|f Investigating the swiveling domain mechanism of the Pyruvate phosphate dikinase (PPDK)
|x 1
536 _ _ |a 553 - Physical Basis of Diseases (POF3-553)
|0 G:(DE-HGF)POF3-553
|c POF3-553
|f POF III
|x 2
588 _ _ |a Dataset connected to CrossRef
700 1 _ |a Gohlke, Holger
|0 P:(DE-Juel1)172663
|b 1
|e Corresponding author
773 _ _ |a 10.1038/s41598-017-08521-w
|g Vol. 7, no. 1, p. 8020
|0 PERI:(DE-600)2615211-3
|n 1
|p 8020
|t Scientific reports
|v 7
|y 2017
|x 2045-2322
856 4 _ |u https://juser.fz-juelich.de/record/837023/files/s41598-017-08521-w.pdf
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/837023/files/s41598-017-08521-w.gif?subformat=icon
|x icon
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/837023/files/s41598-017-08521-w.jpg?subformat=icon-1440
|x icon-1440
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/837023/files/s41598-017-08521-w.jpg?subformat=icon-180
|x icon-180
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/837023/files/s41598-017-08521-w.jpg?subformat=icon-640
|x icon-640
|y OpenAccess
856 4 _ |u https://juser.fz-juelich.de/record/837023/files/s41598-017-08521-w.pdf?subformat=pdfa
|x pdfa
|y OpenAccess
909 C O |o oai:juser.fz-juelich.de:837023
|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)172663
913 1 _ |a DE-HGF
|b Key Technologies
|1 G:(DE-HGF)POF3-510
|0 G:(DE-HGF)POF3-511
|2 G:(DE-HGF)POF3-500
|v Computational Science and Mathematical Methods
|x 0
|4 G:(DE-HGF)POF
|3 G:(DE-HGF)POF3
|l Supercomputing & Big Data
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)POF3-553
|2 G:(DE-HGF)POF3-500
|v Physical Basis of Diseases
|x 1
|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)JSC-20090406
|k JSC
|l Jülich Supercomputing Center
|x 0
920 1 _ |0 I:(DE-Juel1)NIC-20090406
|k NIC
|l John von Neumann - Institut für Computing
|x 1
920 1 _ |0 I:(DE-Juel1)ICS-6-20110106
|k ICS-6
|l Strukturbiochemie
|x 2
980 1 _ |a APC
980 1 _ |a FullTexts
980 _ _ |a journal
980 _ _ |a VDB
980 _ _ |a I:(DE-Juel1)JSC-20090406
980 _ _ |a I:(DE-Juel1)NIC-20090406
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
980 _ _ |a APC
980 _ _ |a UNRESTRICTED
981 _ _ |a I:(DE-Juel1)IBI-7-20200312

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21