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Publication Abstract from PubMed

The Lon proteases are a unique family of chambered proteases with a built-in AAA+ (ATPases associated with diverse cellular activities) module. Here, crystal structures of a unique member of the Lon family with no intrinsic ATPase activity in the proteolytically active form are reported both alone and in complexes with three covalent inhibitors: two peptidomimetics and one derived from a natural product. This work reveals the unique architectural features of an ATP-independent Lon that selectively degrades unfolded protein substrates. Importantly, these results provide mechanistic insights into the recognition of inhibitors and polypeptide substrates within the conserved proteolytic chamber, which may aid the development of specific Lon-protease inhibitors.

Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors.,Liao JH, Ihara K, Kuo CI, Huang KF, Wakatsuki S, Wu SH, Chang CI Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1395-402. doi:, 10.1107/S0907444913008214. Epub 2013 Jul 13. PMID:23897463^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.