2JQY
Outer Membrane Protein G
Summary for 2JQY
| Entry DOI | 10.2210/pdb2jqy/pdb |
| Descriptor | Outer membrane protein G (1 entity in total) |
| Functional Keywords | ompg, membrane protein |
| Biological source | Escherichia coli |
| Cellular location | Cell outer membrane; Multi-pass membrane protein: P76045 |
| Total number of polymer chains | 1 |
| Total formula weight | 32805.33 |
| Authors | Liang, B.,Tamm, L.K. (deposition date: 2007-06-15, release date: 2007-10-09, Last modification date: 2023-12-20) |
| Primary citation | Liang, B.,Tamm, L.K. Structure of outer membrane protein G by solution NMR spectroscopy. Proc.Natl.Acad.Sci.USA, 104:16140-16145, 2007 Cited by PubMed Abstract: The bacterial outer membrane protein G (OmpG), a monomeric pH-gated porin, was overexpressed in Escherichia coli and refolded in beta-octyl glucoside micelles. After transfer into dodecylphosphocholine micelles, the solution structure of OmpG was determined by solution NMR spectroscopy at pH 6.3. Complete backbone assignments were obtained for 234 of 280 residues based on CA, CB, and CO connection pathways determined from a series of TROSY-based 3D experiments at 800 MHz. The global fold of the 14-stranded beta-barrel was determined based on 133 long-range NOEs observed between neighboring strands and local chemical shift and NOE information. The structure of the barrel is very similar to previous crystal structures, but the loops of the solution structure are quite flexible. PubMed: 17911261DOI: 10.1073/pnas.0705466104 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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