Phage Tailspike Proteins with β-Solenoid Fold as Thermostable Carbohydrate Binding Materials

被引：20

作者：

Barbirz, Stefanie ^{[1
]}

Becker, Marion ^{[1
]}

Freiberg, Alexander ^{[1
]}

Seckler, Robert ^{[1
]}

机构：

[1] Univ Potsdam, D-14476 Golm, Germany

来源：

MACROMOLECULAR BIOSCIENCE | 2009年 / 9卷 / 02期

关键词：

biofibers; carbohydrate binding; protein kinetic stability; tailspike; thermal properties; SODIUM DODECYL-SULFATE; CRYSTAL-STRUCTURE; KINETIC STABILITY; ENDORHAMNOSIDASE; MUTATIONS; PATHWAY; HELIX;

D O I：

10.1002/mabi.200800278

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

We have investigated the stability of three tailspike proteins (TSPs) from bacteriophages Sf6, P22, and HK620. Tailspikes are rod-like homotrimers with comparable beta-solenoid folds and similarly high kinetic stability in spite of different amino acid sequences. As tailspikes bind polysaccharides to recognize the bacterial host cell, their stability is required for maintenance of bacteriophage infectivity under harsh extracellular conditions. They resist denaturation by SDS at ambient temperature and their unfolding is slow even in 6 m guanidinium hydrochloride (GdmHCl). This makes them interesting candidates for very stable carbohydrate binding protein materials.

引用

页码：169 / 173

页数：5

共 28 条

[1] Crystal structure of Escherichia coli phage HK620 tailspike:: podoviral tailspike endoglycosidase modules are evolutionarily related [J].