1N5N

Crystal Structure of Peptide Deformylase from Pseudomonas aeruginosa

1N5N の概要

• エントリーDOI: 10.2210/pdb1n5n/pdb
• 関連するPDBエントリー: 1LM4 1LM6 1LME
• 分子名称: Peptide deformylase, ZINC ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: metalloenzyme, drug design, deformylation, hydrolase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42140.74

構造登録者

Kreusch, A.,Spraggon, G.,Lee, C.C.,Klock, H.,McMullan, D.,Ng, K.,Shin, T.,Vincent, J.,Warner, I.,Ericson, C.,Lesley, S.A. (登録日: 2002-11-06, 公開日: 2003-06-24, 最終更新日: 2024-02-14)

主引用文献

Kreusch, A.,Spraggon, G.,Lee, C.C.,Klock, H.,McMullan, D.,Ng, K.,Shin, T.,Vincent, J.,Warner, I.,Ericson, C.,Lesley, S.A.
Structure analysis of peptide deformylases from streptococcus pneumoniae,staphylococcus aureus, thermotoga maritima, and pseudomonas aeruginosa: snapshots of the oxygen sensitivity of peptide deformylase
J.MOL.BIOL., 330:309-321, 2003

PubMed Abstract: Peptide deformylase (PDF) has received considerable attention during the last few years as a potential target for a new type of antibiotics. It is an essential enzyme in eubacteria for the removal of the formyl group from the N terminus of the nascent polypeptide chain. We have solved the X-ray structures of four members of this enzyme family, two from the Gram-positive pathogens Streptococcus pneumoniae and Staphylococcus aureus, and two from the Gram-negative bacteria Thermotoga maritima and Pseudomonas aeruginosa. Combined with the known structures from the Escherichia coli enzyme and the recently solved structure of the eukaryotic deformylase from Plasmodium falciparum, a complete picture of the peptide deformylase structure and function relationship is emerging. This understanding could help guide a more rational design of inhibitors. A structure-based comparison between PDFs reveals some conserved differences between type I and type II enzymes. Moreover, our structures provide insights into the known instability of PDF caused by oxidation of the metal-ligating cysteine residue.

PubMed: 12823970
DOI: 10.1016/S0022-2836(03)00596-5

実験手法

X-RAY DIFFRACTION (1.8 Å)