1bh3: Difference between revisions

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{{STRUCTURE_1bh3|  PDB=1bh3  |  SCENE=  }}  
{{STRUCTURE_1bh3|  PDB=1bh3  |  SCENE=  }}  


'''E1M, A116K MUTANT OF RH. BLASTICA PORIN'''
===E1M, A116K MUTANT OF RH. BLASTICA PORIN===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Pore eyelet mutant]]
[[Category: Pore eyelet mutant]]
[[Category: Porin]]
[[Category: Porin]]
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Revision as of 19:09, 30 June 2008

File:1bh3.png

Template:STRUCTURE 1bh3

E1M, A116K MUTANT OF RH. BLASTICA PORINE1M, A116K MUTANT OF RH. BLASTICA PORIN

Template:ABSTRACT PUBMED 9684893

About this StructureAbout this Structure

1BH3 is a Single protein structure of sequence from Rhodobacter blasticus. Full crystallographic information is available from OCA.

ReferenceReference

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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