5V50

Crystal Structure of MpPR-1i

5V50 の概要

• エントリーDOI: 10.2210/pdb5v50/pdb
• 関連するPDBエントリー: 5V51
• 分子名称: PR-1 protein (2 entities in total)
• 機能のキーワード: pathogenesis-related protein 1, cacao infection, lipid binding protein
• 由来する生物種: Moniliophthora perniciosa (Witches'-broom disease fungus)
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 137195.95

構造登録者

Luo, Z.,Asojo, O. (登録日: 2017-03-12, 公開日: 2017-08-30, 最終更新日: 2024-10-30)

主引用文献

Baroni, R.M.,Luo, Z.,Darwiche, R.,Hudspeth, E.M.,Schneiter, R.,Pereira, G.A.G.,Mondego, J.M.C.,Asojo, O.A.
Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches' Broom Disease of Cacao.
Sci Rep, 7:7818-7818, 2017

PubMed Abstract: The pathogenic fungi Moniliophthora perniciosa causes Witches' Broom Disease (WBD) of cacao. The structure of MpPR-1i, a protein expressed by M. perniciosa when it infects cacao, are presented. This is the first reported de novo structure determined by single-wavelength anomalous dispersion phasing upon soaking with selenourea. Each monomer has flexible loop regions linking the core alpha-beta-alpha sandwich topology that comprise ~50% of the structure, making it difficult to generate an accurate homology model of the protein. MpPR-1i is monomeric in solution but is packed as a high ~70% solvent content, crystallographic heptamer. The greatest conformational flexibility between monomers is found in loops exposed to the solvent channel that connect the two longest strands. MpPR-1i lacks the conserved CAP tetrad and is incapable of binding divalent cations. MpPR-1i has the ability to bind lipids, which may have roles in its infection of cacao. These lipids likely bind in the palmitate binding cavity as observed in tablysin-15, since MpPR-1i binds palmitate with comparable affinity as tablysin-15. Further studies are required to clarify the possible roles and underlying mechanisms of neutral lipid binding, as well as their effects on the pathogenesis of M. perniciosa so as to develop new interventions for WBD.

PubMed: 28798297
DOI: 10.1038/s41598-017-07887-1

実験手法

X-RAY DIFFRACTION (2.43 Å)