Hi all,
E3 ubiquitin ligase is responsible for flagging proteins for degradation by
transferring ubiquitin from a donor protein onto the molecule to be degraded.
It is activated by phosphorylation of a tyrosine which promotes a huge
conformational change, swinging its RING domain 180 degrees to put the
enzyme's two substrates in proximity.
Read more about this enzyme and see the conformational changes happen before
your very own eyes in this latest installment of Quips (QUite Interesting Pdb
Structures; pdbe.org/quips) at:
http://pdbe.org/quips?story=LordCBL
If you have an interesting structure whose story you would like to tell (with
our help) in the form of a Quips article, please contact us at pdbe from ebi.ac.uk
--Gerard
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Gerard J. Kleywegt, PDBe, EMBL-EBI, Hinxton, UK
gerard from ebi.ac.uk ..................... pdbe.org
Secretary: Pauline Haslam pdbe_admin from ebi.ac.uk
