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Maltoporin

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LamB porin
Structure of maltoporin from Salmonella typhimurium.[1]
Identifiers
SymbolLamB
PfamPF02264
InterProIPR003192
SCOP22mpr / SCOPe / SUPFAM
TCDB1.B.3
OPM superfamily32
OPM protein2mpr
CDDcd01346
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1a0sQ:97-505 1oh2R:97-505 1a0tP:97-505

1mprA:28-452 2mprB:28-452 1mpmA:28-446 1mpoC:28-446 1af6A:28-446 1malC:28-446

1mpqB:28-446 1mpnB:28-446

Maltoporins (or LamB porins) are bacterial outer membrane proteins of the porin family. Maltoporin forms a trimeric structure which facilitates the diffusion of maltodextrins across the outer membrane of Gram-negative bacteria. The membrane channel is formed by an antiparallel beta-barrel.[2]

Most pores used for diffusion contain only 16 antiparallel strands, but maltoporin has 18. The structure of maltoporin contains long loops and short turns. The long loops are in contact with the cell exterior and the turns are in contact with the periplasm. This channel is involved in sugar transport. The sugar initially binds to the first greasy residue with van der Waals forces. The sugar continues through the channel by guided diffusion of the sugar along the greasy residues which form a "slide".[3]

Maltoporin's original name was LamB because it is a bacteriophage lambda receptor. This channel is specific for maltosaccharides, whose affinity for the channel increases as the length of the chain increases.[3]

References

[edit]
  1. ^ Meyer JE, Hofnung M, Schulz GE (March 1997). "Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside". J. Mol. Biol. 266 (4): 761–75. doi:10.1006/jmbi.1996.0823. PMID 9102468.
  2. ^ Schirmer T, Rosenbusch JP, Keller TA, Wang YF (1995). "Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution". Science. 267 (5197): 512–514. doi:10.1126/science.7824948. PMID 7824948. S2CID 44587780.
  3. ^ a b Ranquin, An; Van Gelder, Patrick (October 2004). "Maltoporin: sugar for physics and biology". Research in Microbiology. 155 (8): 611–616. doi:10.1016/j.resmic.2004.05.007.