001     139206
005     20210129212458.0
024 7 _ |a 10.1016/j.str.2013.01.017
|2 doi
024 7 _ |a WOS:000317800100004
|2 WOS
024 7 _ |a altmetric:1289839
|2 altmetric
024 7 _ |a pmid:23478063
|2 pmid
037 _ _ |a FZJ-2013-05209
041 _ _ |a English
082 _ _ |a 570
100 1 _ |a Kalisman, N.
|0 P:(DE-HGF)0
|b 0
|e Corresponding author
245 _ _ |a The Crystal Structures of the Eukaryotic Chaperonin CCT Reveal Its Functional Partitioning
260 _ _ |a London [u.a.]
|c 2013
|b Elsevier Science
336 7 _ |a Journal Article
|b journal
|m journal
|0 PUB:(DE-HGF)16
|s 1384421991_6864
|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
500 _ _ |3 POF3_Assignment on 2016-02-29
520 _ _ |a In eukaryotes, CCT is essential for the correct and efficient folding of many cytosolic proteins, most notably actin and tubulin. Structural studies of CCT have been hindered by the failure of standard crystallographic analysis to resolve its eight different subunit types at low resolutions. Here, we exhaustively assess the R value fit of all possible CCT models to available crystallographic data of the closed and open forms with resolutions of 3.8 Å and 5.5 Å, respectively. This unbiased analysis finds the native subunit arrangements with overwhelming significance. The resulting structures provide independent crystallographic proof of the subunit arrangement of CCT and map major asymmetrical features of the particle onto specific subunits. The actin and tubulin substrates both bind around subunit CCT6, which shows other structural anomalies. CCT is thus clearly partitioned, both functionally and evolutionary, into a substrate-binding side that is opposite to the ATP-hydrolyzing side.
536 _ _ |a 452 - Structural Biology (POF2-452)
|0 G:(DE-HGF)POF2-452
|c POF2-452
|x 0
|f POF II
700 1 _ |a Schröder, Gunnar
|0 P:(DE-Juel1)132018
|b 1
|u fzj
700 1 _ |a Levitt, M.
|0 P:(DE-HGF)0
|b 2
773 _ _ |a 10.1016/j.str.2013.01.017
|p 540-549
|n 4
|0 PERI:(DE-600)2031189-8
|t Structure
|v 21
|x 0969-2126
856 4 _ |u http://www.cell.com/structure/abstract/S0969-2126%2813%2900039-7?switch=standard
856 4 _ |u https://juser.fz-juelich.de/record/139206/files/FZJ-2013-05209.pdf
|y Restricted
909 C O |o oai:juser.fz-juelich.de:139206
|p VDB
910 1 _ |a Forschungszentrum Jülich GmbH
|0 I:(DE-588b)5008462-8
|k FZJ
|b 1
|6 P:(DE-Juel1)132018
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
913 1 _ |a DE-HGF
|b Schlüsseltechnologien
|1 G:(DE-HGF)POF2-450
|0 G:(DE-HGF)POF2-452
|2 G:(DE-HGF)POF2-400
|v Structural Biology
|x 0
|4 G:(DE-HGF)POF
|3 G:(DE-HGF)POF2
|l BioSoft
914 1 _ |y 2013
915 _ _ |a Peer review unknown
|0 StatID:(DE-HGF)0040
|2 StatID
915 _ _ |a JCR
|0 StatID:(DE-HGF)0100
|2 StatID
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 DBCoverage
|0 StatID:(DE-HGF)0199
|2 StatID
|b Thomson Reuters Master Journal List
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0200
|2 StatID
|b SCOPUS
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0300
|2 StatID
|b Medline
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0310
|2 StatID
|b NCBI Molecular Biology Database
915 _ _ |a Nationallizenz
|0 StatID:(DE-HGF)0420
|2 StatID
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1030
|2 StatID
|b Current Contents - Life Sciences
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)1050
|2 StatID
|b BIOSIS Previews
920 _ _ |l yes
920 1 _ |0 I:(DE-Juel1)ICS-6-20110106
|k ICS-6
|l Strukturbiochemie
|x 0
980 _ _ |a journal
980 _ _ |a VDB
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)IBI-7-20200312


LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21