1OPF
THE STRUCTURE OF OMPF PORIN IN A TETRAGONAL CRYSTAL FORM
Summary for 1OPF
| Entry DOI | 10.2210/pdb1opf/pdb |
| Descriptor | MATRIX PORIN OUTER MEMBRANE PROTEIN F (1 entity in total) |
| Functional Keywords | membrane protein |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane; Multi-pass membrane protein: P02931 |
| Total number of polymer chains | 6 |
| Total formula weight | 222685.50 |
| Authors | Cowan, S.W.,Schirmer, T.,Pauptit, R.A.,Jansonius, J.N. (deposition date: 1994-11-21, release date: 1995-02-07, Last modification date: 2024-02-14) |
| Primary citation | Cowan, S.W.,Garavito, R.M.,Jansonius, J.N.,Jenkins, J.A.,Karlsson, R.,Konig, N.,Pai, E.F.,Pauptit, R.A.,Rizkallah, P.J.,Rosenbusch, J.P.,Rummel, G.,Schirmer, T. The structure of OmpF porin in a tetragonal crystal form. Structure, 3:1041-1050, 1995 Cited by PubMed Abstract: OmpF porin is a trimeric integral membrane protein responsible for the passive transport of small hydrophilic molecules, such as nutrients and waste products, across the outer membrane of Escherichia coli. Very few membrane proteins have been crystallized in three dimensions, yet this stable protein can be obtained in several crystal forms. Comparison of the structures of the same membrane protein in two different packing environments is of major interest, because it allows us to explore the integrity of the structure outside the natural membrane environment. PubMed: 8589999DOI: 10.1016/S0969-2126(01)00240-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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