6ck7
Crystal structure of a peptide deformylase from Legionella pneumophila bound to actinonin
Structural highlights
FunctionQ5ZSC4_LEGPH Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.[HAMAP-Rule:MF_00163] Publication Abstract from PubMedLegionella pneumophila serogroup 1 is the primary causative agent of Legionnaires' disease, a rare but severe respiratory infection. While the fatality rate of Legionnaires' disease is low in the general population, it is more pronounced in vulnerable communities such as the immunocompromised. Thus, the development of new antimicrobials is of interest for use when existing antibiotics may not be applicable. Peptide deformylases (PDFs) have been under continued investigation as targets for novel antimicrobial compounds. PDF plays an essential role in protein synthesis, removing the N-terminal formyl group from new polypeptides, and is required for growth in most bacteria. Here, we report two crystal structures of L. pneumophila serogroup 1 PDF (LpPDF) bound to either Ni(2+), an active state, or inhibited by actinonin and Zn(2+); the structures were determined to 1.5 and 1.65 A resolution, respectively, and were solved by the Seattle Structural Genomics Center for Infectious Disease (SSGCID). The SSGCID is charged with determining structures of biologically important proteins and molecules from human pathogens. As actinonin is an antimicrobial natural product that has been used as a reference compound in drug development, these structures will help support the ongoing drug-development process. Structures of Legionella pneumophila serogroup 1 peptide deformylase bound to nickel(II) and actinonin.,Nguyen CL, Fan W, Fisher S, Matthews K, Norman JO, Abendroth J, Barrett KF, Craig JK, Edwards TE, Lorimer DD, McLaughlin KJ Acta Crystallogr F Struct Biol Commun. 2025 Apr 1;81(Pt 4):163-170. doi: , 10.1107/S2053230X25001876. Epub 2025 Mar 17. PMID:40091854[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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