2JQ2

NMR structure of the anticoccidial peptide PW2 in DPC micelles

2JQ2 の概要

• エントリーDOI: 10.2210/pdb2jq2/pdb
• 関連するPDBエントリー: 1MO2
• NMR情報: BMRB: 15267
• 分子名称: pw2 (1 entity in total)
• 機能のキーワード: pw2, dpc, membrane, antimicrobial, antimicrobial protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 1613.88

構造登録者

Almeida, F.C.,Tinoco, L.W.,Gomes-Neto, F.,Valente, A.P. (登録日: 2007-05-28, 公開日: 2007-10-16, 最終更新日: 2024-05-08)

主引用文献

Tinoco, L.W.,Gomes-Neto, F.,Valente, A.P.,Almeida, F.C.
Effect of micelle interface on the binding of anticoccidial PW2 peptide
J.Biomol.Nmr, 39:315-322, 2007

PubMed Abstract: PW2 is an anticoccidial peptide active against Eimeria acervulina and Eimeria tenella. We determined the structure of PW2 in dodecylphosphocholine micelles. The structure showed two distinct regions: an amphipathic N-terminal 3(10) helix and an aromatic region containing WWR interface-binding motif. The aromatic region acted as a scaffold of the protein in the interface and shared the same structure in both DPC and SDS micelles. N-terminal helix interacted with DPC but not with SDS interface. Chemical shift change was slow when SDS was added to PW2 in DPC and fast when DPC was added to PW2 in SDS, indicating that interaction with DPC micelles was kinetically more stable than with SDS micelles. Also, DPC interface was able to accommodate PW2, but it maintained the conformational arrangement in the aromatic region observed for SDS micelles. This behavior, which is different from that observed for other antimicrobial peptides with WWR motif, may be associated with the absence of PW2 antibacterial activity and its selectivity for Eimeria parasites.

PubMed: 17926009
DOI: 10.1007/s10858-007-9202-6

実験手法

SOLUTION NMR