5DIR

membrane protein at 2.8 Angstroms

5DIR の概要

• エントリーDOI: 10.2210/pdb5dir/pdb
• 関連するBIRD辞書のPRD_ID: PRD_002257
• 分子名称: Lipoprotein signal peptidase, Globomycin, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (4 entities in total)
• 機能のキーワード: membrane protein, protease, antibiotic, complex, hydrolase
• 由来する生物種: Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 95465.92

構造登録者

Vogeley, L.,El Arnaout, T.,Bailey, J.,Boland, C.,Caffrey, M. (登録日: 2015-09-01, 公開日: 2016-03-02, 最終更新日: 2024-10-09)

主引用文献

Vogeley, L.,El Arnaout, T.,Bailey, J.,Stansfeld, P.J.,Boland, C.,Caffrey, M.
Structural basis of lipoprotein signal peptidase II action and inhibition by the antibiotic globomycin.
Science, 351:876-880, 2016

PubMed Abstract: With functions that range from cell envelope structure to signal transduction and transport, lipoproteins constitute 2 to 3% of bacterial genomes and play critical roles in bacterial physiology, pathogenicity, and antibiotic resistance. Lipoproteins are synthesized with a signal peptide securing them to the cytoplasmic membrane with the lipoprotein domain in the periplasm or outside the cell. Posttranslational processing requires a signal peptidase II (LspA) that removes the signal peptide. Here, we report the crystal structure of LspA from Pseudomonas aeruginosa complexed with the antimicrobial globomycin at 2.8 angstrom resolution. Mutagenesis studies identify LspA as an aspartyl peptidase. In an example of molecular mimicry, globomycin appears to inhibit by acting as a noncleavable peptide that sterically blocks the active site. This structure should inform rational antibiotic drug discovery.

PubMed: 26912896
DOI: 10.1126/science.aad3747

実験手法

X-RAY DIFFRACTION (2.8 Å)