Structural highlights
Function
[LAMB_SALTY] Involved in the transport of maltose and maltodextrins. Does not act as a receptor for phages.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The maltodextrin-specific (malto-)porin from Salmonella typhimurium has been crystallized. Its three-dimensional structure was determined at 2.4 A resolution (1 A = 0.1 nm). A comparison with the structure of the homologous porin from Escherichia coli as well as with the sequences of other related porins showed that there are regions of appreciable sequence and structure variability, despite close overall similarity. The maltoporin structure was analyzed with a bound nitrophenyl-maltotrioside as well as without ligand. Maltotrioside binding had a negligible effect on the polypeptide structure. It binds at the pore eyelet assuming a conformation close to the natural amylose helix.
Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside.,Meyer JE, Hofnung M, Schulz GE J Mol Biol. 1997 Mar 7;266(4):761-75. PMID:9102468[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Meyer JE, Hofnung M, Schulz GE. Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J Mol Biol. 1997 Mar 7;266(4):761-75. PMID:9102468 doi:10.1006/jmbi.1996.0823
