2mqe: Difference between revisions
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The | ==Solution structure of Escherichia coli Outer membrane protein A C-terminal domain== | ||
<StructureSection load='2mqe' size='340' side='right'caption='[[2mqe]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2mqe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_DH1 Escherichia coli DH1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MQE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MQE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 30 models</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mqe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mqe OCA], [https://pdbe.org/2mqe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mqe RCSB], [https://www.ebi.ac.uk/pdbsum/2mqe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mqe ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/OMPA_ECOLI OMPA_ECOLI] Required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. Serves as a receptor for a number of T-even like phages. Also acts as a porin with low permeability that allows slow penetration of small solutes. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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 beta-barrel in the outer membrane. Consequently it was suggested that OmpA is composed of two independently folded domains in which the N-terminal beta-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 (OmpA180-325). 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 OmpA180-325 with the TonB protein. In addition, we have also expressed and purified full-length OmpA (OmpA1-325) 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. | |||
The periplasmic domain of Escherichia coli outer membrane protein A can undergo a localized temperature dependent structural transition.,Ishida H, Garcia-Herrero A, Vogel HJ Biochim Biophys Acta. 2014 Aug 15. pii: S0005-2736(14)00290-9. doi:, 10.1016/j.bbamem.2014.08.008. PMID:25135663<ref>PMID:25135663</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2mqe" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli DH1]] | |||
[[Category: Large Structures]] | |||
[[Category: Ishida H]] | |||
[[Category: Vogel H]] | |||
