1mpr
MALTOPORIN FROM SALMONELLA TYPHIMURIUM
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| , resolution 2.8Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1MPR is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
ReferenceReference
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
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