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6CK7

Crystal structure of a peptide deformylase from Legionella pneumophila bound to actinonin

6CK7 の概要
エントリーDOI10.2210/pdb6ck7/pdb
関連するPDBエントリー6CAZ
分子名称Peptide deformylase, ZINC ION, ACTINONIN, ... (5 entities in total)
機能のキーワードnational institute of allergy and infectious diseases, niaid, structural genomics, legionnaires' disease, formyl-l-methionyl peptide, formate, methionyl peptide, seattle structural genomics center for infectious disease, ssgcid, hydrolase-antibiotic complex, hydrolase/antibiotic
由来する生物種Legionella pneumophila
タンパク質・核酸の鎖数4
化学式量合計83438.84
構造登録者
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2018-02-27, 公開日: 2018-03-07, 最終更新日: 2025-04-09)
主引用文献Nguyen, C.L.,Fan, W.,Fisher, S.,Matthews, K.,Norman, J.O.,Abendroth, J.,Barrett, K.F.,Craig, J.K.,Edwards, T.E.,Lorimer, D.D.,McLaughlin, K.J.
Structures of Legionella pneumophila serogroup 1 peptide deformylase bound to nickel(II) and actinonin.
Acta Crystallogr.,Sect.F, 81:163-170, 2025
Cited by
PubMed Abstract: Legionella 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, an active state, or inhibited by actinonin and Zn; the structures were determined to 1.5 and 1.65 Å 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.
PubMed: 40091854
DOI: 10.1107/S2053230X25001876
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.65 Å)
構造検証レポート
Validation report summary of 6ck7
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-07-23に公開中

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