1GFN
OMPF PORIN DELETION (MUTANT DELTA 109-114)
Summary for 1GFN
| Entry DOI | 10.2210/pdb1gfn/pdb |
| Descriptor | MATRIX PORIN OUTER MEMBRANE PROTEIN F, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (3 entities in total) |
| Functional Keywords | outer membrane, transmembrane protein, porin, membrane protein |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane ; Multi-pass membrane protein : P02931 |
| Total number of polymer chains | 1 |
| Total formula weight | 40110.74 |
| Authors | Lou, K.-L.,Schirmer, T. (deposition date: 1996-05-08, release date: 1996-12-07, Last modification date: 2024-02-07) |
| Primary citation | Lou, K.L.,Saint, N.,Prilipov, A.,Rummel, G.,Benson, S.A.,Rosenbusch, J.P.,Schirmer, T. Structural and functional characterization of OmpF porin mutants selected for larger pore size. I. Crystallographic analysis. J.Biol.Chem., 271:20669-20675, 1996 Cited by PubMed Abstract: OmpF porin is a nonspecific pore protein from the outer membrane of Escherichia coli. Previously, a set of mutants was selected that allow the passage of long maltodextrins that do not translocate through the wild-type pore. Here, we describe the crystal structures of four point mutants and one deletion mutant from this set; their functional characterization is reported in the accompanying paper (Saint, N., Lou, K.-L., Widmer, C., Luckey, M., Schirmer, T., Rosenbusch, J. P. (1996) J. Biol. Chem. 271, 20676-20680). All mutations have a local effect on the structure of the pore constriction and result in a larger pore cross-section. Substitution of each of the three closely packed arginine residues at the pore constriction (Arg-42, Arg-82, and Arg-132) by shorter uncharged residues causes rearrangement of the adjacent basic residues. This demonstrates mutual stabilization of these residues in the wild-type porin. Deletion of six residues from the internal loop (Delta109-114) results in disorder of seven adjacent residues but does not alter the structure of the beta-barrel framework. Thus, the large hollow beta-barrel motif can be regarded as an autonomous structure. PubMed: 8702816DOI: 10.1074/jbc.271.34.20676 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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