6A0Q

The crystal structure of Lpg2622_E64 complex

Summary for 6A0Q

• Entry DOI: 10.2210/pdb6a0q/pdb
• Descriptor: Lpg2622, N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE (3 entities in total)
• Functional Keywords: cysteine protease, hydrolase
• Biological source: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
• Total number of polymer chains: 2
• Total formula weight: 76524.14

Authors

Gong, X.,Ge, H. (deposition date: 2018-06-06, release date: 2018-09-12, Last modification date: 2024-03-27)

Primary citation

Gong, X.,Zhao, X.,Zhang, W.,Wang, J.,Chen, X.,Hameed, M.F.,Zhang, N.,Ge, H.
Structural characterization of the hypothetical protein Lpg2622, a new member of the C1 family peptidases from Legionella pneumophila
FEBS Lett., 592:2798-2810, 2018

PubMed Abstract: 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 β-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.

PubMed: 30071124
DOI: 10.1002/1873-3468.13210

Experimental method

X-RAY DIFFRACTION (2.2 Å)