PMID- 10404219
OWN - NLM
STAT- MEDLINE
DCOM- 19990806
LR  - 20131121
IS  - 1072-8368 (Print)
IS  - 1072-8368 (Linking)
VI  - 6
IP  - 7
DP  - 1999 Jul
TI  - 3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding
      conformation of a type II chaperonin.
PG  - 639-42
AB  - The type II chaperonin CCT (chaperonin containing Tcp-1) of eukaryotic cytosol is
      a heteromeric 16-mer particle composed of eight different subunits.
      Three-dimensional reconstructions of apo-CCT and ATP-CCT have been obtained at 28
      A resolution by cryo-electron microscopy. Binding of ATP generates an asymmetric 
      particle; one ring has a slightly different conformation from the apo-CCT ring,
      while the other has undergone substantial movements in the apical domains. Upon
      ATP binding the apical domains rotate and point towards the cylinder axis, so
      that the helical protrusions present at their tips could act as a lid closing the
      ring cavity.
FAU - Llorca, O
AU  - Llorca O
AD  - Centro Nacional de Biotecnologia, CSIC, Campus Universidad Autonoma de Madrid,
      Spain.
FAU - Smyth, M G
AU  - Smyth MG
FAU - Carrascosa, J L
AU  - Carrascosa JL
FAU - Willison, K R
AU  - Willison KR
FAU - Radermacher, M
AU  - Radermacher M
FAU - Steinbacher, S
AU  - Steinbacher S
FAU - Valpuesta, J M
AU  - Valpuesta JM
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Nat Struct Biol
JT  - Nature structural biology
JID - 9421566
RN  - 0 (Archaeal Proteins)
RN  - 0 (Cct2 protein, Haloferax volcanii)
RN  - 0 (Heat-Shock Proteins)
RN  - 0 (Molecular Chaperones)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
SB  - IM
MH  - Adenosine Triphosphate/*chemistry
MH  - Animals
MH  - *Archaeal Proteins
MH  - Cryoelectron Microscopy
MH  - Heat-Shock Proteins/*chemistry
MH  - Male
MH  - Mice
MH  - Molecular Chaperones/*chemistry
MH  - Protein Binding
MH  - *Protein Conformation
MH  - *Protein Folding
MH  - Testis/chemistry
MH  - Thermoplasma/chemistry
EDAT- 1999/07/15 10:00
MHDA- 2001/03/23 10:01
CRDT- 1999/07/15 10:00
PHST- 1999/07/15 10:00 [pubmed]
PHST- 2001/03/23 10:01 [medline]
PHST- 1999/07/15 10:00 [entrez]
AID - 10.1038/10689 [doi]
PST - ppublish
SO  - Nat Struct Biol. 1999 Jul;6(7):639-42. doi: 10.1038/10689.