FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4327571856> ?p ?o ?g. }

• W4327571856 abstract "The dynamic assembly of actin is controlled by the hydrolysis of ATP, bound to the center of the molecule. Upon polymerization, actin undergoes a conformational change from the monomeric G-form to the fibrous F-form, which is associated with the flipping of the side chain of His161 toward ATP. His161 flipping from the gauche-minus to gauche-plus conformation leads to a rearrangement of the active site water molecules, including ATP attacking water (W1), into an orientation capable of hydrolysis. We previously showed that by using a human cardiac muscle α-actin expression system, mutations in the Pro-rich loop residues (A108G and P109A) and in a residue that was hydrogen-bonded to W1 (Q137A) affect the rate of polymerization and ATP hydrolysis. Here, we report the crystal structures of the three mutant actins bound to AMPPNP or ADP-Pi determined at a resolution of 1.35-1.55 Å, which are stabilized in the F-form conformation with the aid of the fragmin F1 domain. In A108G, His161 remained non-flipped despite the global actin conformation adopting the F-form, demonstrating that the side chain of His161 is flipped to avoid a steric clash with the methyl group of A108. Because of the non-flipped His161, W1 was located away from ATP, similar to G-actin, which was accompanied by incomplete hydrolysis. In P109A, the absence of the bulky proline ring allowed His161 to be positioned near the Pro-rich loop, with a minor influence on ATPase activity. In Q137A, two water molecules replaced the side-chain oxygen and nitrogen of Gln137 almost exactly at their positions; consequently, the active site structure, including the W1 position, is essentially conserved. This seemingly contradictory observation to the reported low ATPase activity of the Q137A filament could be attributed to a high fluctuation of the active site water. Together, our results suggest that the elaborate structural design of the active site residues ensures the precise control of the ATPase activity of actin." @default.
• W4327571856 created "2023-03-17" @default.
• W4327571856 creator A5025325506 @default.
• W4327571856 creator A5041779831 @default.
• W4327571856 creator A5057984567 @default.
• W4327571856 creator A5058058056 @default.
• W4327571856 creator A5091076634 @default.
• W4327571856 date "2023-03-16" @default.
• W4327571856 modified "2023-09-25" @default.
• W4327571856 title "Mutagenic analysis of actin reveals the mechanism of His161 flipping that triggers ATP hydrolysis" @default.
• W4327571856 cites W1966349701 @default.
• W4327571856 cites W1968203524 @default.
• W4327571856 cites W2011658408 @default.
• W4327571856 cites W2020956640 @default.
• W4327571856 cites W2022945133 @default.
• W4327571856 cites W2026064166 @default.
• W4327571856 cites W2035687084 @default.
• W4327571856 cites W2038840577 @default.
• W4327571856 cites W2041933909 @default.
• W4327571856 cites W2050333027 @default.
• W4327571856 cites W2053271991 @default.
• W4327571856 cites W2057477511 @default.
• W4327571856 cites W2059013803 @default.
• W4327571856 cites W2062643184 @default.
• W4327571856 cites W2065283382 @default.
• W4327571856 cites W2081693079 @default.
• W4327571856 cites W2081719547 @default.
• W4327571856 cites W2090521614 @default.
• W4327571856 cites W2105809801 @default.
• W4327571856 cites W2113395636 @default.
• W4327571856 cites W2124026197 @default.
• W4327571856 cites W2140040046 @default.
• W4327571856 cites W2140141405 @default.
• W4327571856 cites W2143480500 @default.
• W4327571856 cites W2146080841 @default.
• W4327571856 cites W2154197653 @default.
• W4327571856 cites W2154465669 @default.
• W4327571856 cites W2162187556 @default.
• W4327571856 cites W2169045417 @default.
• W4327571856 cites W2566481240 @default.
• W4327571856 cites W2798548541 @default.
• W4327571856 cites W2805664184 @default.
• W4327571856 cites W2896922881 @default.
• W4327571856 cites W2900803161 @default.
• W4327571856 cites W2948426268 @default.
• W4327571856 cites W2996148875 @default.
• W4327571856 cites W4248872320 @default.
• W4327571856 cites W4289520791 @default.
• W4327571856 cites W4306641828 @default.
• W4327571856 doi "https://doi.org/10.3389/fcell.2023.1105460" @default.
• W4327571856 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37009486" @default.
• W4327571856 hasPublicationYear "2023" @default.
• W4327571856 type Work @default.
• W4327571856 citedByCount "0" @default.
• W4327571856 crossrefType "journal-article" @default.
• W4327571856 hasAuthorship W4327571856A5025325506 @default.
• W4327571856 hasAuthorship W4327571856A5041779831 @default.
• W4327571856 hasAuthorship W4327571856A5057984567 @default.
• W4327571856 hasAuthorship W4327571856A5058058056 @default.
• W4327571856 hasAuthorship W4327571856A5091076634 @default.
• W4327571856 hasBestOaLocation W43275718561 @default.
• W4327571856 hasConcept C12554922 @default.
• W4327571856 hasConcept C125705527 @default.
• W4327571856 hasConcept C141315368 @default.
• W4327571856 hasConcept C166940927 @default.
• W4327571856 hasConcept C178790620 @default.
• W4327571856 hasConcept C181199279 @default.
• W4327571856 hasConcept C185592680 @default.
• W4327571856 hasConcept C201194858 @default.
• W4327571856 hasConcept C23265538 @default.
• W4327571856 hasConcept C2777339483 @default.
• W4327571856 hasConcept C32909587 @default.
• W4327571856 hasConcept C44228677 @default.
• W4327571856 hasConcept C521977710 @default.
• W4327571856 hasConcept C55493867 @default.
• W4327571856 hasConcept C71240020 @default.
• W4327571856 hasConcept C8010536 @default.
• W4327571856 hasConcept C86803240 @default.
• W4327571856 hasConcept C94412978 @default.
• W4327571856 hasConceptScore W4327571856C12554922 @default.
• W4327571856 hasConceptScore W4327571856C125705527 @default.
• W4327571856 hasConceptScore W4327571856C141315368 @default.
• W4327571856 hasConceptScore W4327571856C166940927 @default.
• W4327571856 hasConceptScore W4327571856C178790620 @default.
• W4327571856 hasConceptScore W4327571856C181199279 @default.
• W4327571856 hasConceptScore W4327571856C185592680 @default.
• W4327571856 hasConceptScore W4327571856C201194858 @default.
• W4327571856 hasConceptScore W4327571856C23265538 @default.
• W4327571856 hasConceptScore W4327571856C2777339483 @default.
• W4327571856 hasConceptScore W4327571856C32909587 @default.
• W4327571856 hasConceptScore W4327571856C44228677 @default.
• W4327571856 hasConceptScore W4327571856C521977710 @default.
• W4327571856 hasConceptScore W4327571856C55493867 @default.
• W4327571856 hasConceptScore W4327571856C71240020 @default.
• W4327571856 hasConceptScore W4327571856C8010536 @default.
• W4327571856 hasConceptScore W4327571856C86803240 @default.
• W4327571856 hasConceptScore W4327571856C94412978 @default.
• W4327571856 hasFunder F4320334764 @default.
• W4327571856 hasLocation W43275718561 @default.
• W4327571856 hasLocation W43275718562 @default.

• next