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1.B.3 The Sugar Porin (SP) Family

The SP family includes the well characterized maltoporin of E. coli for which the three-dimensional structures with and without its substrate have been obtained by X-ray diffraction. The protein consists of an 18 β-stranded β-barrel in contrast to proteins of the general bacterial porin family (GBP) and the Rhodobacter PorCa Porin (RPP) family which consist of 16 β-stranded &beta-barrels. Although maltoporin contains a wider beta-barrel than the porins of the GBP and RPP families (TC#s 1.B.1 and 1.B.7), it exhibits a narrower channel, showing only 5% of the ionic conductance of the latter porins.

References associated with 1.B.3 family:

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Nelson, B.R., C.A. Makarewich, D.M. Anderson, B.R. Winders, C.D. Troupes, F. Wu, A.L. Reese, J.R. McAnally, X. Chen, E.T. Kavalali, S.C. Cannon, S.R. Houser, R. Bassel-Duby, and E.N. Olson. (2016). Muscle physiology. A peptide encoded by a transcript annotated as long noncoding RNA enhances SERCA activity in muscle. Science 351: 271-275. 26816378
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Schirmer, T., T.A. Keller, Y.F. Wang and J.P. Rosenbusch (1995). Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267: 512-514.
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Wang, Y.F., R. Dutzler, P.J. Rizkallah, J.P. Rosenbusch and T. Schirmer (1997). Channel specificity: structural basis for sugar discrimination and differential flux rates in maltoporin. J. Mol. Biol. 272: 56-63. 9299337