Matches in SemOpenAlex for { <https://semopenalex.org/work/W2080617276> ?p ?o ?g. }
Showing items 1 to 79 of
79
with 100 items per page.
- W2080617276 endingPage "571a" @default.
- W2080617276 startingPage "571a" @default.
- W2080617276 abstract "Hsp70 chaperones play important roles in cells including protein folding, trafficking, degradation and enabling survival under stress conditions. DnaK is an E. coli Hsp70 homolog comprising an ATPase domain and a substrate-binding domain. DnaK has two substrate-affinity states: ATP binding lowers the affinity of the substrate, whereas its hydrolysis leads to a higher affinity of substrate for binding. ATP-dependent communication between the two domains is essential for chaperone function and mediated via a conserved hydrophobic linker (384GDVKDVLLL392). Previous studies showed that when the linker interacts with the ATPase domain, which was studied by the construct containing the entire linker, DnaK(1-392), an enhanced ATPase rate is observed compared to the construct lacking the conserved 389VLLL392 linker region, DnaK(1-388). This observation suggests that structural rearrangements caused by linker docking adopt the ATPase domain in a closed conformation, leading to an enhanced, pH-dependent ATPase activity. Here, our aim is to delineate the residues that are responsible for the linker induced conformational rearrangements. In that line, using molecular dynamic simulations we identified a putative network of interactions through Arg71-Glu81-Asp85-Thr225-His226 at the lobe interface of the ATPase domain that might be critical in stabilization of the domain in the so called “open” and “closed” conformational equilibrium. We made point mutations for these sites on the two ATPase domain constructs, and studied the structural and functional effects of these residues on the ATPase domain as a function of pH using various biophysical and biochemical methods. Mutations' effects studied by equilibrium thermodynamic measurements showed variations for the constructs, but dramatic changes were observed in the dynamics of the constructs. Our results suggest the linker as a controller for ATPase domain dynamics changes partly through the identified network." @default.
- W2080617276 created "2016-06-24" @default.
- W2080617276 creator A5004161432 @default.
- W2080617276 creator A5022594396 @default.
- W2080617276 creator A5024565251 @default.
- W2080617276 creator A5026386935 @default.
- W2080617276 creator A5056073479 @default.
- W2080617276 creator A5067321055 @default.
- W2080617276 date "2013-01-01" @default.
- W2080617276 modified "2023-10-17" @default.
- W2080617276 title "A Putative Network of Interactions Controls the Opening and Closing Dynamics of the ATPase Domain of E. Coli Hsp70, DNAk" @default.
- W2080617276 doi "https://doi.org/10.1016/j.bpj.2012.11.3169" @default.
- W2080617276 hasPublicationYear "2013" @default.
- W2080617276 type Work @default.
- W2080617276 sameAs 2080617276 @default.
- W2080617276 citedByCount "0" @default.
- W2080617276 crossrefType "journal-article" @default.
- W2080617276 hasAuthorship W2080617276A5004161432 @default.
- W2080617276 hasAuthorship W2080617276A5022594396 @default.
- W2080617276 hasAuthorship W2080617276A5024565251 @default.
- W2080617276 hasAuthorship W2080617276A5026386935 @default.
- W2080617276 hasAuthorship W2080617276A5056073479 @default.
- W2080617276 hasAuthorship W2080617276A5067321055 @default.
- W2080617276 hasBestOaLocation W20806172761 @default.
- W2080617276 hasConcept C104317684 @default.
- W2080617276 hasConcept C111919701 @default.
- W2080617276 hasConcept C113027372 @default.
- W2080617276 hasConcept C12554922 @default.
- W2080617276 hasConcept C141315368 @default.
- W2080617276 hasConcept C142724271 @default.
- W2080617276 hasConcept C166342909 @default.
- W2080617276 hasConcept C167625842 @default.
- W2080617276 hasConcept C181199279 @default.
- W2080617276 hasConcept C185592680 @default.
- W2080617276 hasConcept C23265538 @default.
- W2080617276 hasConcept C2775962898 @default.
- W2080617276 hasConcept C2780557392 @default.
- W2080617276 hasConcept C41008148 @default.
- W2080617276 hasConcept C55493867 @default.
- W2080617276 hasConcept C71924100 @default.
- W2080617276 hasConcept C86803240 @default.
- W2080617276 hasConceptScore W2080617276C104317684 @default.
- W2080617276 hasConceptScore W2080617276C111919701 @default.
- W2080617276 hasConceptScore W2080617276C113027372 @default.
- W2080617276 hasConceptScore W2080617276C12554922 @default.
- W2080617276 hasConceptScore W2080617276C141315368 @default.
- W2080617276 hasConceptScore W2080617276C142724271 @default.
- W2080617276 hasConceptScore W2080617276C166342909 @default.
- W2080617276 hasConceptScore W2080617276C167625842 @default.
- W2080617276 hasConceptScore W2080617276C181199279 @default.
- W2080617276 hasConceptScore W2080617276C185592680 @default.
- W2080617276 hasConceptScore W2080617276C23265538 @default.
- W2080617276 hasConceptScore W2080617276C2775962898 @default.
- W2080617276 hasConceptScore W2080617276C2780557392 @default.
- W2080617276 hasConceptScore W2080617276C41008148 @default.
- W2080617276 hasConceptScore W2080617276C55493867 @default.
- W2080617276 hasConceptScore W2080617276C71924100 @default.
- W2080617276 hasConceptScore W2080617276C86803240 @default.
- W2080617276 hasIssue "2" @default.
- W2080617276 hasLocation W20806172761 @default.
- W2080617276 hasOpenAccess W2080617276 @default.
- W2080617276 hasPrimaryLocation W20806172761 @default.
- W2080617276 hasRelatedWork W1972770744 @default.
- W2080617276 hasRelatedWork W1999268424 @default.
- W2080617276 hasRelatedWork W1999815303 @default.
- W2080617276 hasRelatedWork W2057754968 @default.
- W2080617276 hasRelatedWork W2080617276 @default.
- W2080617276 hasRelatedWork W2326250436 @default.
- W2080617276 hasRelatedWork W2800776875 @default.
- W2080617276 hasRelatedWork W2976101942 @default.
- W2080617276 hasRelatedWork W3034547421 @default.
- W2080617276 hasRelatedWork W3154389764 @default.
- W2080617276 hasVolume "104" @default.
- W2080617276 isParatext "false" @default.
- W2080617276 isRetracted "false" @default.
- W2080617276 magId "2080617276" @default.
- W2080617276 workType "article" @default.