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A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis.

1994; Springer Nature; Volume: 13; Issue: 19 Linguagem: Inglês

10.1002/j.1460-2075.1994.tb06790.x

1460-2075

Phillip E. Klebba, Maurice Hofnung, Alain Charbit,

Bone and Dental Protein Studies

Research Article3 October 1994free access A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis. P.E. Klebba P.E. Klebba Unité de Programmation Moleculaire et Toxicologie Génétique CNRS URA 1444, Institut Pasteur, Paris, France. Search for more papers by this author M. Hofnung M. Hofnung Unité de Programmation Moleculaire et Toxicologie Génétique CNRS URA 1444, Institut Pasteur, Paris, France. Search for more papers by this author A. Charbit A. Charbit Unité de Programmation Moleculaire et Toxicologie Génétique CNRS URA 1444, Institut Pasteur, Paris, France. Search for more papers by this author P.E. Klebba P.E. Klebba Unité de Programmation Moleculaire et Toxicologie Génétique CNRS URA 1444, Institut Pasteur, Paris, France. Search for more papers by this author M. Hofnung M. Hofnung Unité de Programmation Moleculaire et Toxicologie Génétique CNRS URA 1444, Institut Pasteur, Paris, France. Search for more papers by this author A. Charbit A. Charbit Unité de Programmation Moleculaire et Toxicologie Génétique CNRS URA 1444, Institut Pasteur, Paris, France. Search for more papers by this author Author Information P.E. Klebba1, M. Hofnung1 and A. Charbit1 1Unité de Programmation Moleculaire et Toxicologie Génétique CNRS URA 1444, Institut Pasteur, Paris, France. The EMBO Journal (1994)13:4670-4675https://doi.org/10.1002/j.1460-2075.1994.tb06790.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info LamB facilitates the uptake of maltose and maltodextrins across the bacterial outer membrane and acts as a general porin for small molecules. Using directed deletion mutagenesis we removed several regions of the LamB polypeptide and identified a polypeptide loop that both constricts the maltoporin channel and binds maltodextrins. In conjunction with a second sugar binding site that we identified at the rim of the channel, these data clarify, for the first time, the mechanism of transport through a substrate-specific porin. Furthermore, unlike the transverse loops of general porins, which originate from a central location in their primary structure, the loop that regulates LamB permeability originates from a C-terminal site. Thus LamB represents a second distinct class of porins in the bacterial outer membrane that is differently organized and separately evolved from OmpF-type, general porins. Previous ArticleNext Article Volume 13Issue 191 October 1994In this issue RelatedDetailsLoading ...