2prn: Difference between revisions

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|PDB= 2prn |SIZE=350|CAPTION= <scene name='initialview01'>2prn</scene>, resolution 1.93&Aring;
|PDB= 2prn |SIZE=350|CAPTION= <scene name='initialview01'>2prn</scene>, resolution 1.93&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>
|LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2prn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2prn OCA], [http://www.ebi.ac.uk/pdbsum/2prn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2prn RCSB]</span>
}}
}}


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[[Category: Schmid, B.]]
[[Category: Schmid, B.]]
[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
[[Category: C8E]]
[[Category: MG]]
[[Category: integral membrane protein]]
[[Category: integral membrane protein]]
[[Category: pore eyelet mutant]]
[[Category: pore eyelet mutant]]
[[Category: porin]]
[[Category: porin]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:16:34 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:39:48 2008''

Revision as of 04:39, 31 March 2008

File:2prn.jpg


PDB ID 2prn

Drag the structure with the mouse to rotate
, resolution 1.93Å
Ligands: ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



RHODOPSEUDOMONAS BLASTICA PORIN, TRIPLE MUTANT E1M, E99W, A116W


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

2PRN 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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