Sandbox Reserved 1644: Difference between revisions

The Lon proteolytic domain has a highly '''conserved structure'''. Like its orthologues, namely the eubacterium ''[https://fr.wikipedia.org/wiki/Escherichia_coli E. coli]'' ([https://proteopedia.org/wiki/index.php/1rre 1rre]), and the two archaea ''[https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii M. jannaschii]'' and ''[https://fr.wikipedia.org/wiki/Archaeoglobus_fulgidus A. fulgidus]'', it presents at its C-terminal a '''Ser-Lys dyad''' responsible of the substrate degradation activity. Although ''h''LonP active site resembles mostly to the one of ''Ec''LonP, the b5-sheet is replaced by an '''extension to a2'''. Thus, the N-terminal region of this helix carries the catalytic serine is a [https://en.wikipedia.org/wiki/310_helix 3(10) helix] and not a b-strand. As a consequence, ''h''LonP has the ability to bring the Asp852 into the active site to '''close''' it by forming a hydrogen bond with Lys898, a property already observed in ''Mj''Lon active site. This inactive state likely makes the catalytic serine inaccessible to the substrate and constraints the pKa of the lysine. Other main structural differences are '''loop shifts''' connecting the secondary structure elements b1 and b2, and a1.

This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.