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2MQE

Solution structure of Escherichia coli Outer membrane protein A C-terminal domain

Summary for 2MQE
Entry DOI10.2210/pdb2mqe/pdb
NMR InformationBMRB: 25030
DescriptorOmpA domain protein transmembrane region-containing protein (1 entity in total)
Functional Keywordsouter membrane protein a, ompa, membrane protein
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight15712.67
Authors
Ishida, H.,Vogel, H. (deposition date: 2014-06-19, release date: 2014-09-03, Last modification date: 2024-11-20)
Primary citationIshida, H.,Garcia-Herrero, A.,Vogel, H.J.
The periplasmic domain of Escherichia coli outer membrane protein A can undergo a localized temperature dependent structural transition.
Biochim.Biophys.Acta, 1838:3014-3024, 2014
Cited by
PubMed Abstract: Gram-negative bacteria such as Escherichia coli are surrounded by two membranes with a thin peptidoglycan (PG)-layer located in between them in the periplasmic space. The outer membrane protein A (OmpA) is a 325-residue protein and it is the major protein component of the outer membrane of E. coli. Previous structure determinations have focused on the N-terminal fragment (residues 1-171) of OmpA, which forms an eight stranded transmembrane β-barrel in the outer membrane. Consequently it was suggested that OmpA is composed of two independently folded domains in which the N-terminal β-barrel traverses the outer membrane and the C-terminal domain (residues 180-325) adopts a folded structure in the periplasmic space. However, some reports have proposed that full-length OmpA can instead refold in a temperature dependent manner into a single domain forming a larger transmembrane pore. Here, we have determined the NMR solution structure of the C-terminal periplasmic domain of E. coli OmpA (OmpA(180-325)). Our structure reveals that the C-terminal domain folds independently into a stable globular structure that is homologous to the previously reported PG-associated domain of Neisseria meningitides RmpM. Our results lend credence to the two domain structure model and a PG-binding function for OmpA, and we could indeed localize the PG-binding site on the protein through NMR chemical shift perturbation experiments. On the other hand, we found no evidence for binding of OmpA(180-325) with the TonB protein. In addition, we have also expressed and purified full-length OmpA (OmpA(1-325)) to study the structure of the full-length protein in micelles and nanodiscs by NMR spectroscopy. In both membrane mimetic environments, the recombinant OmpA maintains its two domain structure that is connected through a flexible linker. A series of temperature-dependent HSQC experiments and relaxation dispersion NMR experiments detected structural destabilization in the bulge region of the periplasmic domain of OmpA above physiological temperatures, which may induce dimerization and play a role in triggering the previously reported larger pore formation.
PubMed: 25135663
DOI: 10.1016/j.bbamem.2014.08.008
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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