2mpr

MALTOPORIN FROM SALMONELLA TYPHIMURIUMMALTOPORIN FROM SALMONELLA TYPHIMURIUM

Structural highlights 2mpr is a 3 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: , , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin 3D structures

spinqualitylabelsall models 2mpr, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image