Mechanism of maltodextrin transport through LamB
Mechanism of maltodextrin transport through LamB
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DOI：
10.1016/s0923-2508(02)01340-2
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发表时间：
2002-09-01
影响因子：
2.6
通讯作者：
Klebba, PE
中科院分区：
文献类型：
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作者：
Klebba, PE
革兰氏阴性细菌外膜包含几个独立的、生化上不同的转运系统，用于从环境中获取溶质。孔蛋白超家族内存在三种或更多不同类别的膜蛋白，促进糖、氨基酸、核苷酸、维生素和金属的摄取。尽管在过去十年中对这些蛋白质转运蛋白进行了晶体学描述，但孔蛋白催化溶质内化的机制仍存在争议，并且在某些情况下仍然模糊。多年来，Maurice Hofnung 的研究致力于解释 LamB（也称为麦芽孔蛋白）对麦芽糖和麦芽糖糊精的转运。在最近晶体结构的影响下，他的工作帮助勾勒出外膜运输生理学的不同图景，这是对莫里斯开创的强大遗传方法的致敬。这些数据表明麦芽孔蛋白识别麦芽糖糊精的主要决定因素源自其表面环中芳香族氨基酸的构型。 (C) 2002 年科学与医学版 Elsevier SAS。版权所有。
The Gram-negative bacterial outer membrane contains several independent, biochemically distinct transport systems for the acquisition of solutes from the environment. Three or more different classes of membrane proteins exist within the porin superfamily, that facilitate the uptake of sugars, amino acids, nucleotides, vitamins and metals. In spite of crystallographic descriptions of these protein transporters over the past decade, the mechanisms by which porins catalyze solute internalization are controversial, and in some cases still obscure. For many years the research of Maurice Hofnung endeavored to explain the transport of maltose and maltodextrins by LamB, also known as maltoporin. In the shadow of recent crystal structures, his work helped outline a different picture of outer membrane transport physiology, that is a tribute to the powerful genetic approaches Maurice pioneered. These data suggest that the principal determinant of maltodextrin recognition by maltoporin derives from the configuration of aromatic amino acids in its surface loops. (C) 2002 Editions scientifiques et medicales Elsevier SAS. All rights reserved.