Is this the active enzyme or an inactive mutant? does your substrate have any similarity with PEG (size, conformation, bulk etc?) would you assume that if there was a substrate bound to the active site and say a few waters, and/or metal ions it would probably fill the space which in this case PEG is taking.
I think it would be more work, but the best way would be to try to crystallize a inactive mutant with very less change in the active site residues with the substrate( or active enzyme with an analog) and see if the PEG is displaced. ivan On Fri, Feb 19, 2010 at 3:42 AM, Marek Frischerkase < [email protected]> wrote: > Hello, > sorry for my off topic question. > I found a PEG molecule bound to the active site of my enzyme structure. And > I did not expected it there, though I used PEG as precipitant in the > crystallization condition. Now I'm wondering how could bind PEG with its > hydrophobic nature at all in the hydrophobic active site? It seems that the > PEG molecule interacts predominantly with Tryptophans (distance 3.8 A). Did > anybody observe similar cases? And which kind of interaction should there be > active? I would be grateful for your help, > > cheers, > > Marek > > __________________________________________________ > Do You Yahoo!? > Sie sind Spam leid? Yahoo! Mail verfügt über einen herausragenden Schutz > gegen Massenmails. > http://mail.yahoo.com >
