1H6S
Asymmetric conductivity of engineered proteins
Summary for 1H6S
| Entry DOI | 10.2210/pdb1h6s/pdb |
| Related | 1BH3 1PRN 2PRN 3PRN 5PRN 6PRN 7PRN 8PRN |
| Descriptor | PORIN (1 entity in total) |
| Functional Keywords | membrane protein, integral membrane protein porin |
| Biological source | RHODOPSEUDOMONAS BLASTICA |
| Total number of polymer chains | 1 |
| Total formula weight | 32222.72 |
| Authors | Bannwarth, M.,Schulz, G.E. (deposition date: 2001-06-22, release date: 2002-12-12, Last modification date: 2023-12-13) |
| Primary citation | Bannwarth, M.,Schulz, G.E. Asymmetric Conductivity of Engineered Porins Protein Eng., 15:799-, 2002 Cited by PubMed Abstract: Positively charged peptide segments of 16 and 18 residues were inserted at a periplasmic turn of the porin from Rhodobacter blasticus in order to form an electric field-dependent plug. The X-ray diffraction analysis of a mutant confirmed that the structure of the porin had remained intact and that the insert was mobile. Incorporation experiments of single molecules into lipid bilayers showed that the distribution of electric conduction increments depended on the field polarity. The observed distributions are explained if the porin molecules enter the bilayer preferentially with their periplasmic surface first. Furthermore, the conduction of membrane-incorporated porin mutants changed reproducibly on field reversal showing asymmetries of reverse similar 15%, while the wild-type remained constant. This asymmetry is most likely caused by the electric field pressing the charged insert onto the pore eyelet in one field direction and removing it from the eyelet in the other. The results encourage attempts to improve the inserts in order to eventually reach diode characteristics. PubMed: 12468713DOI: 10.1093/PROTEIN/15.10.799 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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