4V8R

The crystal structures of the eukaryotic chaperonin CCT reveal its functional partitioning

This is a non-PDB format compatible entry.

Summary for 4V8R

• Entry DOI: 10.2210/pdb4v8r/pdb
• Related: 4B2T
• Descriptor: T-COMPLEX PROTEIN 1 SUBUNIT ALPHA, BERYLLIUM TRIFLUORIDE ION, MAGNESIUM ION, ... (11 entities in total)
• Functional Keywords: chaperone
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Total number of polymer chains: 32
• Total formula weight: 1952737.22

Authors

Kalisman, N.,Schroder, G.F.,Levitt, M. (deposition date: 2012-03-28, release date: 2014-07-09, Last modification date: 2024-05-08)

Primary citation

Kalisman, N.,Schroder, G.F.,Levitt, M.
The Crystal Structures of the Eukaryotic Chaperonin Cct Reveal its Functional Partitioning
Structure, 21:540-, 2013

PubMed Abstract: 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.

PubMed: 23478063
DOI: 10.1016/J.STR.2013.01.017

Experimental method

X-RAY DIFFRACTION (3.8 Å)