Re: [ccp4bb] Na-Binding Protein?

The human branched-chain alpha-ketoacid dehydrogenase requires a K+ ion to stabilize the binding of the cofactor thiamine diphosphate and to achieve maximum catalytic efficiency. See https://www.ncbi.nlm.nih.gov/pubmed/10745006 Diana ** Diana R.

Re: [ccp4bb] Na-Binding Protein?

That's very interesting. I guess it's an unusual manifestation of the Hofmeister series. It might give guidance to developers of screens for both crystallization and cryoEM. Thx, Patrick On 9 January 2018 at 15:44, Andrew Mesecar wrote: > Dear Jacob, > > > > One of my

Re: [ccp4bb] Na-Binding Protein?

Dear Jacob, The protease thrombin is another example. Thrombin is activated by Na+ (but not Li+ or K+). We have shown using NMR that Na+ binding allosterically stabilizes active conformations of thrombin. Additionally, numerous crystal structures of Na+-free (“slow” thrombin) and Na+-bound

Re: [ccp4bb] Na-Binding Protein?

Dear Jacob, One of my favorite examples of monovalent cation discrimination is by the enzyme Pyruvate Kinase. It prefers K(+), NH4(+), Rb(+) and Tl+ for maximum catalysis and then activity falls off as the monovalent cation sizes get larger, Cs(+) or smaller Na(+) >> Li (+). The conformations

Re: [ccp4bb] Na-Binding Protein?

Hi Jacob, Ion-channel and receptor folks have been working on these types of questions... see: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2629458/ if you are looking for a model system, perhaps engineer a version of calmodulin that is specific for Na+ rather than Ca++?  Perhaps someone