A cluster of charged and aromatic residues in the C-terminal portion of maltoporin participates in sugar binding and uptake

Molecular and General Genetics

Volumn 260, Issue 2-3, 1998, Pages 185-192

  Charbit, A ^a   Wang, J ^a,b   Michel, V ^a   Hofnung, M ^a  

^a CNRS   (France)

^b BEIJING INSTITUTE OF BIOTECHNOLOGY   (China)

Author keywords

Antibiotic sensitivity; LamB; Maltoside transport; Specific porin

Indexed keywords

ALANINE; BACITRACIN; DEXTRIN; MALTODEXTRIN; MALTOSE; OUTER MEMBRANE PROTEIN; PORIN; SUGAR; VANCOMYCIN;

AMINO ACID SUBSTITUTION; ANTIBIOTIC SENSITIVITY; ARTICLE; BACTERIAL OUTER MEMBRANE; ESCHERICHIA COLI K 12; MEMBRANE TRANSPORT; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANTI-BACTERIAL AGENTS; BACITRACIN; BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIOPHAGES; BIOLOGICAL TRANSPORT; DRUG RESISTANCE, MICROBIAL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MALTOSE; MEMBRANE TRANSPORT PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OLIGOSACCHARIDES; POLYSACCHARIDES; RECEPTORS, VIRUS; VANCOMYCIN;

BACTERIA (MICROORGANISMS); ESCHERICHIA; ESCHERICHIA COLI K12;

EID: 0031736256     PISSN: 00268925     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004380050884     Document Type: Article

References (27)

1. Ausubel FM, Brent R, Kingston RE, Moore D, Smith JA, Seidman JG, Struhl K (eds) (1990) Current protocols in molecular biology, Wiley Interscience, New York
2. Benz R, Maier E, Gentschev I (1993) TolC of Escherichia coli functions as an outer membrane channel. Zentralbl Bakeriol 278:187-196
3. Boulain JC, Charbit A, Hofnung M (1986) Mutagenesis by random linker insertion into the lamB gene of E. coli K12. Mol Gen Genet 205:339-348
4. Charbit A, Gehring K, Nikaido H, Ferenci T, Hofnung M (1988) Maltose transport and starch binding in phage-resistant point mutants of maltoporin: functional and topological implications. J Mol Biol 201:487-496
5. Charbit A, Werts C, Michel V, Klebba PE, Quillardet P, Hofnung M (1994) A role of residue 151 of LamB in bacteriophage lambda adorption : possible steric effect of amino acid substitutions. J Bacteriol 176:3204-3209
6. Clément JM, Lepouce E, Marchal C, Hofnung M (1983) Genetic study of a membrane protein: DNA sequence alterations due to 17 lamB point mutations affecting adsorption of phage lambda. EMBO J 2:77-80
7. Cowan SW, Schirmer T, Rummel G, Steiert M, Ghosh R, Pauptit RA, Jansonius JN, Rosenbusch JP (1992) Crystal structures explain functional properties of two E. coli porins. Nature 358:727-733
8. Desaymard C, Debarbouillé M, Jolit M, Schwartz M (1986) Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli. EMBO J 5:1383-1388
9. Ferenci T, Boos W (1980) The role of the Escherichia coli lambda receptor in the transport of maltose and maltodextrins. J Supramol Struct 13:101-116
10. Ferenci T, Lee KS (1982) Directed evolution of the lambda receptor of Escherichia coli through affinity chromotography selection. J Mol Biol 160: 431-444
11. Forst D, Welte W, Wacker T, Diederichs K (1998) Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nature Struct Biol 5:37-46
12. Freundlieb S, Ehmann U, Boos W (1988) Facilitated diffusion of p-nitrophenyl-α-D-maltohexaoside through the outer membrane of Escherichia coli. J Biol Chem 263:314-320
13. Gabay J, Schwartz M (1982) Monoclonal antibodies as a probe for structure and function of Escherichia coli outer membrane protein. J Biol Chem 257:6627-6630
14. Hofnung M (1995) An intelligent channel (and more). Science 267: 473-474
15. Jordy M, Andersen C, Schulein K, Ferenci T, Benz R (1996) Rate constants of sugar transport through two LamB mutants of Escherichia coli: comparison with wild-type maltoporin and LamB of Salmonella typhimurium. J Mol Biol 259:666-678
16. Klebba PE, Hofnung M, Charbit A (1994) A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis. EMBO J 13:4670-4675
17. Klebba PE, Newton SMC, Charbit A, Michel V, Perrin D, Hofnung M (1997) Further genetic analysis of the C-terminal external loop region in Escherichia coli maltoporin. Res Microbiol 148:375-387
18. Kreusch A, Neubüser A, Schiltz E, Weckesser J, Schulz GE (1994) Structure of the membrane channel porin from Rhodopseudomas blastica at 2.0 Å resolution. Protein Sci 3:58-63
19. Newton SMC, Klebba PE, Michel V, Hofnung M, Charbit A (1996) Topology of the membrane protein LamB by epitope tagging and a comparison with the X-ray model. J Bacteriol 178:3447-3456
20. Nikaido H, Vaara M (1985) Molecular basis of bacterial outer membrane permeability. FEMS Microbiol Rev 49:1-32
21. Schirmer T, Keller T, Wang YF, Rosenbush JP (1995) Structural basis for sugar translocation through maltoporin channels at 3.5 Å resolution. Science 267:512-514
22. Schülein K, Andersen C, Benz R (1995) The deletion of 70 amino acids near the N-terminal end of the sucrose porin Scry causes its functional similarity to LamB in vivo and in vitro. Mol Microbiol 17:757-767
23. Szmelcman S, Hofnung M (1975) Maltose transport in Escherichia coli K12. Involvement of the bacteriophage lambda receptor. J Bacteriol 124:112-118
24. Vyas NK (1991) Atomic features of protein-carbohydrate interactions. Curr Opin Struct Biol 1:732-740
25. Wandersman C, Létoffé S (1993) Involvement of lipopolysaccharide in the secretion of Escherichia coli α-haemolysin and Erwinia chrisanthemi proteases. Mol Microbiol 7:141-150
26. Weiss MS, Kreusch A, Schiltz E, Nestel U, Welte W, Weckesser J, Schulz GE (1991) The structure of porin from Rhodobacter capsulatus at 1.8 Åresolution. FEBS Lett 280:379-382
27. Werts C, Michel V, Hofnung M, Charbit A (1994) Adsorption of bacteriophage lambda on the LamB protein of E. coli K12: point mutations in gene J of lambda responsible for extended host range. J Bacteriol 176:941-947