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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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Dutzler, R., Y.F. Wang, P.J. Rizkallah, J.P. Rosenbusch and T. Schirmer (1996). Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 4: 127-134. 8805519
Hardesty, C., C. Ferran and J.M. DiRenzo (1991). Plasmid-mediated sucrose metabolism in Escherichia coli: characterization of scrY, the structural gene for a phosphoenolpyruvate-dependent sucrose phosphotransferase system outer membrane porin. J. Bacteriol. 173: 449-456. 1846143
Jeanteur, D., J.H. Lakey and F. Pattus (1991). The bacterial porin superfamily: sequence alignment and structure prediction. Mol. Microbiol. 5: 2153-2164. 1662760
Jeanteur, D., J.H. Lakey and F. Pattus (1994). The porin superfamily: diversity and common features. In: Bacterial Cell Wall. Edited by Ghuysen, J.M., Hakenbeck, R. Elsevier, Amsterdam, pp. 363-380.
Kim, B.H., C. Andersen, J. Kreth, C. Ulmke, K. Schmid, and R. Benz. (2002). Site-directed mutagenesis within the central constriction site of ScrY (sucroseporin): effect on ion transport and comparison of maltooligosaccharide binding to LamB of Escherichia coli. J. Membr. Biol. 187: 239-253. 12163981
Lin, X.M., M.J. Yang, H. Li, C. Wang, and X.X. Peng. (2014). Decreased expression of LamB and Odp1 complex is crucial for antibiotic resistance in Escherichia coli. J Proteomics 98: 244-253. 24412198
Löwe, H., P. Sinner, A. Kremling, and K. Pflüger-Grau. (2018). Engineering sucrose metabolism in Pseudomonas putida highlights the importance of porins. Microb Biotechnol. [Epub: Ahead of Print] 29808622
Meyer, J.E.W., M. Hofnung and G.E. Schulz (1997). Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J. Mol. Biol. 266: 761-775. 9102468
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
Nikaido, H. (1992). Porins and specific channels of bacterial outer membranes. Mol. Microbiol. 6: 435-442. 1373213
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.
Schulz, G.E. (1996). Porins: general to specific, native to engineered passive pores. Curr. Opin. Struc. Biol. 6: 485-490. 8794162
Sun, L., F. Bertelshofer, G. Greiner, and R.A. Böckmann. (2016). Characteristics of Sucrose Transport through the Sucrose-Specific Porin ScrY Studied by Molecular Dynamics Simulations. Front Bioeng Biotechnol 4: 9. 26913282
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