1bh3: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1bh3.jpg|left|200px]] | [[Image:1bh3.jpg|left|200px]] | ||
'''E1M, A116K MUTANT OF RH. BLASTICA PORIN''' | {{Structure | ||
|PDB= 1bh3 |SIZE=350|CAPTION= <scene name='initialview01'>1bh3</scene>, resolution 2.19Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''E1M, A116K MUTANT OF RH. BLASTICA PORIN''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1BH3 is a [ | 1BH3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_blasticus Rhodobacter blasticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BH3 OCA]. | ||
==Reference== | ==Reference== | ||
Porin mutants with new channel properties., Schmid B, Maveyraud L, Kromer M, Schulz GE, Protein Sci. 1998 Jul;7(7):1603-11. PMID:[http:// | Porin mutants with new channel properties., Schmid B, Maveyraud L, Kromer M, Schulz GE, Protein Sci. 1998 Jul;7(7):1603-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9684893 9684893] | ||
[[Category: Rhodobacter blasticus]] | [[Category: Rhodobacter blasticus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 21: | Line 30: | ||
[[Category: porin]] | [[Category: porin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:10:55 2008'' | ||
Revision as of 11:10, 20 March 2008
| |||||||
| , resolution 2.19Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 10:10:55 2008