9qft

Crystal structure of Def2 in complex with actinonin

spinqualitylabelsall models 9qft, resolution 1.82Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9qft is a 2 chain structure with sequence from Vibrio cholerae O1 biovar El Tor str. N16961. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.82Å Ligands: BB2, NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DEF2_VIBCH 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 (By similarity). Publication Abstract from PubMed Peptide deformylases (PDFs) are enzymes that are essential for bacterial viability and attractive targets for antibiotic development. Yet, despite their conserved function, many bacteria encode multiple PDFs, a genomic feature whose prevalence and implications remain largely unexplored. Here, we reveal that nearly half of all bacterial genomes carry more than one PDF gene, frequently embedded within mobile genetic elements such as plasmids and integrons. In Vibrio cholerae, the accessory PDF (Def2VCH) confers reduced susceptibility to actinonin (ACT), the most studied PDF inhibitor, while still supporting bacterial growth in the absence of the canonical PDF copies (Def1VCH). Crystallographic analysis shows that this reduced susceptibility stems from an arginine-to-tyrosine substitution that probably reduces ACT binding. Strikingly, this resistance signature is shared by integron-encoded PDFs, and transfer of an integron-encoded PDF cassette from Pseudoxanthomonas into a susceptible V. cholerae is sufficient to abolish ACT susceptibility. These findings reveal a hidden reservoir of resistance within the bacterial mobilome and shed light on potential mechanisms of bacterial resilience to environmental PDF inhibitors. Unraveling the Prevalence and Multifaceted Roles of Accessory Peptide Deformylases in Bacterial Adaptation and Resistance.,Lamberioux M, Ducos-Galand M, Kaminski PA, Littner E, Betton JM, Mechaly A, Haouz A, Mazel D Mol Biol Evol. 2025 Nov 28;42(12):msaf311. doi: 10.1093/molbev/msaf311. PMID:41316864 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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