3PRN

E1M, A104W MUTANT OF RH. BLASTICA PORIN

Summary for 3PRN

• Entry DOI: 10.2210/pdb3prn/pdb
• Descriptor: PORIN, MAGNESIUM ION, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (4 entities in total)
• Functional Keywords: integral membrane protein, porin, pore eyelet mutant, membrane protein
• Biological source: Rhodobacter blasticus
• Cellular location: Cell outer membrane; Multi-pass membrane protein: P39767
• Total number of polymer chains: 1
• Total formula weight: 31669.69

Authors

Maveyraud, L.,Schmid, B.,Schulz, G.E. (deposition date: 1998-06-12, release date: 1998-08-12, Last modification date: 2024-05-22)

Primary citation

Schmid, B.,Maveyraud, L.,Kromer, M.,Schulz, G.E.
Porin mutants with new channel properties.
Protein Sci., 7:1603-1611, 1998

PubMed Abstract: 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.

PubMed: 9684893

Experimental method

X-RAY DIFFRACTION (1.9 Å)