Dear Gina,
We have recently solved a structure of the glucosamine 6P synthase from E.coli
(GlmS) and surpringsly, although the whole protein was present in this crystal
form, no electron density was observed for the glutaminase domain (240 residues
out of 600), indicating its mobility.
Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B.
Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate
synthase promotes sugar ring opening and formation of the ammonia channel.
J Mol Biol. 2008 Apr 4;377(4):1174-85. Epub 2008 Feb 4.
PMID: 18295797
This domain mobility is functionally essential for the catalysis. Although this
domain is mobile in the absence of ligand, it is ordered in two previous
structures solved in an active and inactive conformation:
- In the inactive conformation, its glutaminase domain was resolved in
the density but the density was very poor. Analysis of the TLS parameters shown
large anisotropic displacements.
- In the active conformation with its glutaminase domain well ordered
but in a different conformation (21 degrees rotation).
Mouilleron S, Golinelli-Pimpaneau B.
Domain motions of glucosamine-6P synthase: comparison of the anisotropic
displacements in the crystals and the catalytic hinge-bending rotation.
Protein Sci. 2007 Mar;16(3):485-93.
PMID: 17322533
Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B.
Glutamine binding opens the ammonia channel and activates glucosamine-6P
synthase.
J Biol Chem. 2006 Feb 17;281(7):4404-12. Epub 2005 Dec 9.
PMID: 16339762
I hope it will help you,
Cheers
Stephane
-------- Message d'origine--------
De: CCP4 bulletin board de la part de Gina Clayton
Date: sam. 28/06/2008 23:30
À: [email protected]
Objet : [ccp4bb] Disordered domains in crystal strutures
Dear CCP4ers
can anyone recommend papers describing crystal structures of proteins
with a large functionally important disordered domain or domains.
Thanks in advance
Gina
