1JKZ

NMR Solution Structure of Pisum sativum defensin 1 (Psd1)

1JKZ の概要

• エントリーDOI: 10.2210/pdb1jkz/pdb
• 分子名称: DEFENSE-RELATED PEPTIDE 1 (1 entity in total)
• 機能のキーワード: plant defensin, cys-rich, antifungal, antifungal protein
• 由来する生物種: Pisum sativum (pea)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5217.92

構造登録者

Almeida, M.S.,Cabral, K.M.S.,Kurtenbach, E.,Almeida, F.C.L.,Valente, A.P. (登録日: 2001-07-13, 公開日: 2002-02-06, 最終更新日: 2024-10-30)

主引用文献

Almeida, M.S.,Cabral, K.M.,Kurtenbach, E.,Almeida, F.C.,Valente, A.P.
Solution structure of Pisum sativum defensin 1 by high resolution NMR: plant defensins, identical backbone with different mechanisms of action.
J.Mol.Biol., 315:749-757, 2002

PubMed Abstract: Pisum sativum defensin 1 (Psd1) is a 46 amino acid residue plant defensin isolated from seeds of pea. The three-dimensional structure in solution of Psd1 was determined by two-dimensional NMR data recorded at 600 MHz. Experimental restraints were used for structure calculation using CNS and torsion-angle molecular dynamics. The 20 lowest energy structures were selected and further subjected to minimization, giving a root-mean-square deviation of 0.78(+/- 0.22) A in the backbone and 1.91(+/-0.60) A for over all atoms of the molecule. The protein has a globular fold with a triple-stranded antiparalell beta-sheet and an alpha-helix (from residue Asn17 to Leu27). Psd1 presents the so called "cysteine stabilized alpha/beta motif" and presents identical three-dimensional topology in the backbone with other defensins and neurotoxins. Comparison of the electrostatic surface potential among proteins with high three-dimensional (selected using the softwares TOP and DALI) topology gave insights into the mode of action of Psd1. The surface topologies between proteins that present antifungal activity or sodium channel inhibiting activity are different. On the other hand the surface topology presents several common features with potassium channel inhibitors, suggesting that Psd1 presents this activity. Other common features with potassium channel inhibitors were found including the presence of a lysine residue essential for inhibitory activity. The identity of Psd1 in primary sequence is not enough to infer a mechanism of action, in contrast with the strategy proposed here.

PubMed: 11812144
DOI: 10.1006/jmbi.2001.5252

実験手法

SOLUTION NMR