1UOY

The bubble protein from Penicillium brevicompactum Dierckx exudate.

1UOY の概要

• エントリーDOI: 10.2210/pdb1uoy/pdb
• 分子名称: BUBBLE PROTEIN (2 entities in total)
• 機能のキーワード: exudate protein, sulfur phasing, potential killer toxin
• 由来する生物種: PENICILLIUM BREVICOMPACTUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6579.13

構造登録者

Olsen, J.G.,Flensburg, C.,Olsen, O.,Seibold, M.,Bricogne, G.,Henriksen, A. (登録日: 2003-09-26, 公開日: 2003-11-04, 最終更新日: 2024-10-23)

主引用文献

Olsen, J.G.,Flensburg, C.,Olsen, O.,Bricogne, G.,Henriksen, A.
Solving the Structure of the Bubble Protein Using the Anomalous Sulfur Signal from Single-Crystal in-House Cu Kalpha Diffraction Data Only
Acta Crystallogr.,Sect.D, 60:250-, 2004

PubMed Abstract: A small cysteine-rich protein, the function of which remains elusive, was discovered in the exudate of a Penicillium species. Crystal diffraction experiments conducted using in-house Cu Kalpha radiation and an R-AXIS IV++ imaging-plate detector yielded high-quality data to 1.4 A, with a distinguishable anomalous signal from sulfur (DeltaF/F = 0.031). This was used to phase the data and solve the structure using a single data set; the 64-residue amino-acid sequence was unambiguously determined from the electron density. It revealed a globular all-beta protein with a hitherto unknown fold, having a surface electrostatic charge distribution that is similar to that of another small secreted fungal protein, the Williopsis mrakii killer toxin. Aligning the charge distribution superimposed the potential recognition sites of the two proteins, suggesting a similar negatively charged target.

PubMed: 14747700
DOI: 10.1107/S0907444903025927

実験手法

X-RAY DIFFRACTION (1.5 Å)