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Publication Abstract from PubMed

The Legionella pneumophila type II secretion system can promote bacterial growth under a wide variety of conditions and mediates the secretion of more than 25 proteins, including the uncharacterized effector Lpg2622. Here, we determined the crystal structures of apo-Lpg2622 and Lpg2622 in complex with the cysteine protease inhibitor E64. Structural analysis suggests that Lpg2622 belongs to the C1 family peptidases. Interestingly, unlike the other structurally resolved papain-like cysteine proteases, the propeptide of Lpg2622 forms a novel super-secondary structural fold (hairpin-turn-helix) and can be categorized into a new group. In addition, the N-terminal beta-sheet of the Lpg2622 propeptide plays a regulatory role on enzymatic activity. This study enhances our understanding of the classification and regulatory mechanisms of the C1 family peptidases.

Structural characterization of the hypothetical protein Lpg2622, a new member of the C1 family peptidases from Legionella pneumophila.,Gong X, Zhao X, Zhang W, Wang J, Chen X, Hameed MF, Zhang N, Ge H FEBS Lett. 2018 Aug;592(16):2798-2810. doi: 10.1002/1873-3468.13210. Epub 2018, Aug 20. PMID:30071124^[1]

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