1MPR

MALTOPORIN FROM SALMONELLA TYPHIMURIUM

Summary for 1MPR

• Entry DOI: 10.2210/pdb1mpr/pdb
• Descriptor: MALTOPORIN, CALCIUM ION (3 entities in total)
• Functional Keywords: membrane protein, sugar transport, specific porin, beta barrel
• Biological source: Salmonella typhimurium
• Cellular location: Cell outer membrane; Multi-pass membrane protein: P26466
• Total number of polymer chains: 3
• Total formula weight: 144233.68

Authors

Meyer, J.E.W.,Schulz, G.E. (deposition date: 1996-12-18, release date: 1997-03-12, Last modification date: 2024-10-16)

Primary citation

Meyer, J.E.,Hofnung, M.,Schulz, G.E.
Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside.
J.Mol.Biol., 266:761-775, 1997

PubMed Abstract: 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.

PubMed: 9102468
DOI: 10.1006/jmbi.1996.0823

Experimental method

X-RAY DIFFRACTION (2.8 Å)