FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1986665696> ?p ?o ?g. }

• W1986665696 endingPage "3024" @default.
• W1986665696 startingPage "3014" @default.
• W1986665696 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 (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." @default.
• W1986665696 created "2016-06-24" @default.
• W1986665696 creator A5000514546 @default.
• W1986665696 creator A5024274003 @default.
• W1986665696 creator A5042190192 @default.
• W1986665696 date "2014-12-01" @default.
• W1986665696 modified "2023-10-18" @default.
• W1986665696 title "The periplasmic domain of Escherichia coli outer membrane protein A can undergo a localized temperature dependent structural transition" @default.
• W1986665696 cites W115149147 @default.
• W1986665696 cites W1496063460 @default.
• W1986665696 cites W1507753089 @default.
• W1986665696 cites W1525806299 @default.
• W1986665696 cites W1551519167 @default.
• W1986665696 cites W1560081729 @default.
• W1986665696 cites W1568288844 @default.
• W1986665696 cites W1577922858 @default.
• W1986665696 cites W1580476862 @default.
• W1986665696 cites W1587073004 @default.
• W1986665696 cites W1607188212 @default.
• W1986665696 cites W1650832331 @default.
• W1986665696 cites W1902714978 @default.
• W1986665696 cites W1965600386 @default.
• W1986665696 cites W1966981270 @default.
• W1986665696 cites W1967641814 @default.
• W1986665696 cites W1974737447 @default.
• W1986665696 cites W1975943954 @default.
• W1986665696 cites W1981267913 @default.
• W1986665696 cites W1996764065 @default.
• W1986665696 cites W2001490774 @default.
• W1986665696 cites W2002195659 @default.
• W1986665696 cites W2003599432 @default.
• W1986665696 cites W2004252276 @default.
• W1986665696 cites W2004696942 @default.
• W1986665696 cites W2005034781 @default.
• W1986665696 cites W2005574282 @default.
• W1986665696 cites W2006223771 @default.
• W1986665696 cites W2009918551 @default.
• W1986665696 cites W2012531991 @default.
• W1986665696 cites W2013475505 @default.
• W1986665696 cites W2017518542 @default.
• W1986665696 cites W2022058405 @default.
• W1986665696 cites W2024088027 @default.
• W1986665696 cites W2025431751 @default.
• W1986665696 cites W203285984 @default.
• W1986665696 cites W2037842354 @default.
• W1986665696 cites W2042303206 @default.
• W1986665696 cites W2058646563 @default.
• W1986665696 cites W2060088451 @default.
• W1986665696 cites W2061379882 @default.
• W1986665696 cites W2062557777 @default.
• W1986665696 cites W2071149151 @default.
• W1986665696 cites W2074398530 @default.
• W1986665696 cites W2075286202 @default.
• W1986665696 cites W2080348258 @default.
• W1986665696 cites W2081482228 @default.
• W1986665696 cites W2082176639 @default.
• W1986665696 cites W2093968495 @default.
• W1986665696 cites W2097730526 @default.
• W1986665696 cites W2099054032 @default.
• W1986665696 cites W2100257913 @default.
• W1986665696 cites W2102153468 @default.
• W1986665696 cites W2104176117 @default.
• W1986665696 cites W2107217578 @default.
• W1986665696 cites W2108247880 @default.
• W1986665696 cites W2108616134 @default.
• W1986665696 cites W2112418305 @default.
• W1986665696 cites W2114305625 @default.
• W1986665696 cites W2115230101 @default.
• W1986665696 cites W2120061656 @default.
• W1986665696 cites W2127177253 @default.
• W1986665696 cites W2128517590 @default.
• W1986665696 cites W2130688334 @default.
• W1986665696 cites W2138590891 @default.
• W1986665696 cites W2139040250 @default.
• W1986665696 cites W2145189347 @default.
• W1986665696 cites W2152608798 @default.
• W1986665696 cites W2168747862 @default.
• W1986665696 cites W2169821755 @default.
• W1986665696 cites W2170671445 @default.
• W1986665696 cites W2171348868 @default.
• W1986665696 cites W2172087640 @default.
• W1986665696 cites W41179907 @default.
• W1986665696 cites W4210417723 @default.
• W1986665696 doi "https://doi.org/10.1016/j.bbamem.2014.08.008" @default.
• W1986665696 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25135663" @default.
• W1986665696 hasPublicationYear "2014" @default.
• W1986665696 type Work @default.
• W1986665696 sameAs 1986665696 @default.
• W1986665696 citedByCount "42" @default.
• W1986665696 countsByYear W19866656962015 @default.
• W1986665696 countsByYear W19866656962016 @default.
• W1986665696 countsByYear W19866656962017 @default.
• W1986665696 countsByYear W19866656962018 @default.
• W1986665696 countsByYear W19866656962020 @default.
• W1986665696 countsByYear W19866656962021 @default.
• W1986665696 countsByYear W19866656962022 @default.
• W1986665696 countsByYear W19866656962023 @default.
• W1986665696 crossrefType "journal-article" @default.

• next