TY  - JOUR
AU  - Kalisman, N.
AU  - Schröder, Gunnar
AU  - Levitt, M.
TI  - The Crystal Structures of the Eukaryotic Chaperonin CCT Reveal Its Functional Partitioning
JO  - Structure
VL  - 21
IS  - 4
SN  - 0969-2126
CY  - London [u.a.]
PB  - Elsevier Science
M1  - FZJ-2013-05209
SP  - 540-549
PY  - 2013
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000317800100004
C6  - pmid:23478063
DO  - DOI:10.1016/j.str.2013.01.017
UR  - https://juser.fz-juelich.de/record/139206
ER  -