Sökning: onr:"swepub:oai:DiVA.org:umu-187197" > Dynamic Connection ...
Fältnamn | Indikatorer | Metadata |
---|---|---|
000 | 03595naa a2200397 4500 | |
001 | oai:DiVA.org:umu-187197 | |
003 | SwePub | |
008 | 210908s2021 | |||||||||||000 ||eng| | |
024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1871972 URI |
024 | 7 | a https://doi.org/10.1021/acs.biochem.1c002212 DOI |
040 | a (SwePub)umu | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a ref2 swepub-contenttype |
072 | 7 | a art2 swepub-publicationtype |
100 | 1 | a Ojeda-May, Pedrou Umeå universitet,Kemiska institutionen,Högpresterande beräkningscentrum norr (HPC2N)4 aut0 (Swepub:umu)peoj0002 |
245 | 1 0 | a Dynamic Connection between Enzymatic Catalysis and Collective Protein Motions |
264 | c 2021-07-12 | |
264 | 1 | b American Chemical Society (ACS),c 2021 |
338 | a print2 rdacarrier | |
520 | a Enzymes employ a wide range of protein motions to achieve efficient catalysis of chemical reactions. While the role of collective protein motions in substrate binding, product release, and regulation of enzymatic activity is generally understood, their roles in catalytic steps per se remain uncertain. Here, molecular dynamics simulations, enzyme kinetics, X-ray crystallography, and nuclear magnetic resonance spectroscopy are combined to elucidate the catalytic mechanism of adenylate kinase and to delineate the roles of catalytic residues in catalysis and the conformational change in the enzyme. This study reveals that the motions in the active site, which occur on a time scale of picoseconds to nanoseconds, link the catalytic reaction to the slow conformational dynamics of the enzyme by modulating the free energy landscapes of subdomain motions. In particular, substantial conformational rearrangement occurs in the active site following the catalytic reaction. This rearrangement not only affects the reaction barrier but also promotes a more open conformation of the enzyme after the reaction, which then results in an accelerated opening of the enzyme compared to that of the reactant state. The results illustrate a linkage between enzymatic catalysis and collective protein motions, whereby the disparate time scales between the two processes are bridged by a cascade of intermediate-scale motion of catalytic residues modulating the free energy landscapes of the catalytic and conformational change processes. | |
650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
700 | 1 | a Ul Mushtaq, Ameequ Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)amul0005 |
700 | 1 | a Rogne, Peru Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)pero0018 |
700 | 1 | a Verma, Apoorvu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)apve0002 |
700 | 1 | a Ovchinnikov, Victor4 aut |
700 | 1 | a Grundström, Christinu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)chgr0001 |
700 | 1 | a Dulko-Smith, Beata4 aut |
700 | 1 | a Sauer, Uwe H.u Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)uwsa0001 |
700 | 1 | a Wolf-Watz, Magnus,d 1971-u Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)maswoz04 |
700 | 1 | a Nam, Kwangho4 aut |
710 | 2 | a Umeå universitetb Kemiska institutionen4 org |
773 | 0 | t Biochemistryd : American Chemical Society (ACS)g 60:28, s. 2246-2258q 60:28<2246-2258x 0006-2960x 1520-4995 |
856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-187197 |
856 | 4 8 | u https://doi.org/10.1021/acs.biochem.1c00221 |
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