2mpr
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(New page: 200px<br /><applet load="2mpr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2mpr, resolution 2.4Å" /> '''MALTOPORIN FROM SALMO...)
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Revision as of 10:38, 21 November 2007
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MALTOPORIN FROM SALMONELLA TYPHIMURIUM
Overview
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 Structure
2MPR is a Single protein structure of sequence from Salmonella typhimurium with CA as ligand. Full crystallographic information is available from OCA.
Reference
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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