1bh3
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(New page: 200px<br /><applet load="1bh3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bh3, resolution 2.19Å" /> '''E1M, A116K MUTANT OF...)
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Revision as of 09:32, 20 November 2007
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E1M, A116K MUTANT OF RH. BLASTICA PORIN
Overview
The general diffusion porin from Rhodopseudomonas blastica was produced in, large amounts in Escherichia coli inclusion bodies and (re)natured to the, exact native structure. Here, we report on 13 mutants at the pore eyelet, giving rise to new diffusion properties as measured in planar lipid, bilayer experiments. The crystal structures of seven of these mutants were, established. The effects of charge-modifying mutations at the pore eyelet, are consistent with the known selectivity for cations. Deletions of 16 and, 27 residues of the constriction loop L3 resulted in labile trimers and, pores. The reduction of the eyelet cross section by introducing, tryptophans gave rise to a closely correlated decrease of the, conductivities. A mutant with six newly introduced tryptophans in the, eyelet closed its pore in a defined manner within seconds under a voltage, of 20 mV, suggesting the existence of two states. The results indicate, that the pore can be engineered in a rational manner.
About this Structure
1BH3 is a Single protein structure of sequence from Rhodobacter blasticus with C8E as ligand. Full crystallographic information is available from OCA.
Reference
Porin mutants with new channel properties., Schmid B, Maveyraud L, Kromer M, Schulz GE, Protein Sci. 1998 Jul;7(7):1603-11. PMID:9684893
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