4ab3 | pdb_00004ab3
From Proteopedia
ATP-triggered molecular mechanics of the chaperonin GroEL
Template:ABSTRACT PUBMED 22445172
Function
[CH60_ECOLI] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]
About this Structure
4ab3 is a 14 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
See Also
Reference
- Clare DK, Vasishtan D, Stagg S, Quispe J, Farr GW, Topf M, Horwich AL, Saibil HR. ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin. Cell. 2012 Mar 30;149(1):113-23. Epub 2012 Mar 22. PMID:22445172 doi:10.1016/j.cell.2012.02.047
