5prn
From Proteopedia
(New page: 200px<br /><applet load="5prn" size="450" color="white" frame="true" align="right" spinBox="true" caption="5prn, resolution 2.0Å" /> '''E1M, Y96W, S119W MUTA...) |
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| - | [[Image:5prn.gif|left|200px]]<br /><applet load="5prn" size=" | + | [[Image:5prn.gif|left|200px]]<br /><applet load="5prn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="5prn, resolution 2.0Å" /> | caption="5prn, resolution 2.0Å" /> | ||
'''E1M, Y96W, S119W MUTANT OF RH. BLASTICA PORIN'''<br /> | '''E1M, Y96W, S119W MUTANT OF RH. BLASTICA PORIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The general diffusion porin from Rhodopseudomonas blastica was produced in | + | 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== | ||
| - | 5PRN 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:// | + | 5PRN 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=5PRN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Maveyraud, L.]] | [[Category: Maveyraud, L.]] | ||
[[Category: Schmid, B.]] | [[Category: Schmid, B.]] | ||
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E.]] |
[[Category: C8E]] | [[Category: C8E]] | ||
[[Category: integral membrane protein]] | [[Category: integral membrane protein]] | ||
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[[Category: porin]] | [[Category: porin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:41 2008'' |
Revision as of 17:15, 21 February 2008
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E1M, Y96W, S119W 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
5PRN is a Single protein structure of sequence from Rhodobacter blasticus with 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
Page seeded by OCA on Thu Feb 21 19:15:41 2008
