2ZFG
Structure of OMPF PORIN
Summary for 2ZFG
| Entry DOI | 10.2210/pdb2zfg/pdb |
| Descriptor | Outer membrane protein F, MAGNESIUM ION, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (4 entities in total) |
| Functional Keywords | ompf porin, ordered waters, ion transport, membrane, outer membrane, phage recognition, transmembrane, transport, 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 | 37751.43 |
| Authors | Cramer, W.A.,Zakharov, S.D.,Yamashita, E. (deposition date: 2008-01-04, release date: 2008-07-29, Last modification date: 2023-11-01) |
| Primary citation | Yamashita, E.,Zhalnina, M.V.,Zakharov, S.D.,Sharma, O.,Cramer, W.A. Crystal structures of the OmpF porin: function in a colicin translocon. Embo J., 27:2171-2180, 2008 Cited by PubMed Abstract: The OmpF porin in the Escherichia coli outer membrane (OM) is required for the cytotoxic action of group A colicins, which are proposed to insert their translocation and active domains through OmpF pores. A crystal structure was sought of OmpF with an inserted colicin segment. A 1.6 A OmpF structure, obtained from crystals formed in 1 M Mg2+, has one Mg2+ bound in the selectivity filter between Asp113 and Glu117 of loop 3. Co-crystallization of OmpF with the unfolded 83 residue glycine-rich N-terminal segment of colicin E3 (T83) that occludes OmpF ion channels yielded a 3.0 A structure with inserted T83, which was obtained without Mg2+ as was T83 binding to OmpF. The incremental electron density could be modelled as an extended poly-glycine peptide of at least seven residues. It overlapped the Mg2+ binding site obtained without T83, explaining the absence of peptide binding in the presence of Mg2+. Involvement of OmpF in colicin passage through the OM was further documented by immuno-extraction of an OM complex, the colicin translocon, consisting of colicin E3, BtuB and OmpF. PubMed: 18636093DOI: 10.1038/emboj.2008.137 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.59 Å) |
Structure validation
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