1bh3: Difference between revisions

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New page: left|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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[[Image:1bh3.jpg|left|200px]]<br /><applet load="1bh3" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1bh3.jpg|left|200px]]<br /><applet load="1bh3" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1bh3, resolution 2.19&Aring;" />
caption="1bh3, resolution 2.19&Aring;" />
'''E1M, A116K MUTANT OF RH. BLASTICA PORIN'''<br />
'''E1M, A116K MUTANT OF RH. BLASTICA PORIN'''<br />


==Overview==
==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.
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==
==About this Structure==
1BH3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_blasticus Rhodobacter blasticus] with C8E as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BH3 OCA].  
1BH3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_blasticus Rhodobacter blasticus] with <scene name='pdbligand=C8E:'>C8E</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH3 OCA].  


==Reference==
==Reference==
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[[Category: Maveyraud, L.]]
[[Category: Maveyraud, L.]]
[[Category: Schmid, B.]]
[[Category: Schmid, B.]]
[[Category: Schulz, G.E.]]
[[Category: Schulz, G E.]]
[[Category: C8E]]
[[Category: C8E]]
[[Category: integral membrane protein]]
[[Category: integral membrane protein]]
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[[Category: porin]]
[[Category: porin]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:13 2008''

Revision as of 12:55, 21 February 2008

File:1bh3.jpg


1bh3, resolution 2.19Å

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E1M, A116K MUTANT OF RH. BLASTICA PORIN

OverviewOverview

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 StructureAbout this Structure

1BH3 is a Single protein structure of sequence from Rhodobacter blasticus with as ligand. 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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