Sandbox Reserved 1644: Difference between revisions
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== Evolutionary conservation == | == Evolutionary conservation == | ||
The Lon proteolytic domain has a highly conserved structure. Like its orthologues, namely the eubacterium E. coli (1rre), and the two archaea M. jannaschii and A. fulgidus, it presents at its C-terminal a Ser-Lys dyad responsible of the substrate degradation activity. Although hLonP active site resembles mostly to the one of EcLonP, the b5-sheet is replaced by an extension to a2. Thus, the N-terminal region of this helix carries the catalytic serine is a 310 helix and not a b-strand. As a consequence, hLonP 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 MjLon active site. This inactive state likely makes the catalytic serine inaccessible to the substrate and constraints the pKa of the lysine. Other main structure differences are loops shifts connecting the secondary structure elements b1 and b2, and a1. | |||
== Disease == | == Disease == | ||
