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LcnD的拓扑结构，一种与乳酸乳球菌中细菌素运输有关的蛋白质。

Topology of LcnD, a protein implicated in the transport of bacteriocins from Lactococcus lactis.

作者信息

Franke C M, Leenhouts K J, Haandrikman A J, Kok J, Venema G, Venema K

机构信息

Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan, Haren, The Netherlands.

出版信息

J Bacteriol. 1996 Mar;178(6):1766-9. doi: 10.1128/jb.178.6.1766-1769.1996.

DOI:10.1128/jb.178.6.1766-1769.1996
PMID:8626308
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC177865/
Abstract

Four in-frame translational fusions to both the reporter proteins beta-galactosidase and alkaline phosphatase support a topological model of LcnD, a protein implicated in the transport of several bacteriocins from Lactococcus lactis, in which the N-terminal part is located intracellularly and one transmembrane helix spans the cytoplasmic membrane.

摘要

与报告蛋白β-半乳糖苷酶和碱性磷酸酶的四个读码框内翻译融合支持了LcnD的拓扑模型，LcnD是一种与乳酸乳球菌中几种细菌素的运输有关的蛋白质，其中N端部分位于细胞内，一个跨膜螺旋跨越细胞质膜。

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