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A genetically engineered protein domain binding to bacterial murein, archaeal pseudomurein, and fungal chitin cell wall material

机译:基因改造的蛋白质结构域,可与细菌壁蛋白,古细菌拟壁蛋白和真菌几丁质细胞壁材料结合

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摘要

The major murein and pseudomurein cell wall-binding domains, i.e., the Lysin Motif (LysM) (Pfam PF01476) and pseudomurein cell wall-binding (PMB) (Pfam PF09373) motif, respectively, were genetically fused. The fusion protein is capable of binding to both murein- and pseudomurein-containing cell walls. In addition, it also binds to chitin, the major polymer of fungal cell walls. Binding is influenced by pH and occurs at a pH close to the pI of the binding protein. Functional studies on truncated versions of the fusion protein revealed that murein and chitin binding is provided by the LysM domain, while binding to pseudomurein is achieved through the PMB domain.
机译:主要的壁膜蛋白和伪壁膜蛋白细胞壁结合结构域,即赖氨酸基序(LysM)(Pfam PF01476)和伪壁膜蛋白细胞壁结合(PMB)(Pfam PF09373)基序被基因融合。融合蛋白能够结合含壁粘连蛋白和伪壁连蛋白的细胞壁。此外,它还与几丁质结合,几丁质是真菌细胞壁的主要聚合物。结合受pH影响,并在接近结合蛋白的pI的pH下发生。对融合蛋白截短形式的功能研究表明,LysM结构域提供了鼠莫来汀和几丁质的结合,而通过PMB域则实现了对拟鼠莫来酸的结合。

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