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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004195naa a2200505 4500
001oai:DiVA.org:uu-363422
003SwePub
008181018s2018 | |||||||||||000 ||eng|
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3634222 URI
0247 a https://doi.org/10.1038/s41467-018-06305-y2 DOI
040 a (SwePub)uu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Hong, Nan-Sooku Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia4 aut
2451 0a The evolution of multiple active site configurations in a designed enzyme
264 c 2018-09-25
264 1b Nature Publishing Group,c 2018
338 a electronic2 rdacarrier
520 a Developments in computational chemistry, bioinformatics, and laboratory evolution have facilitated the de novo design and catalytic optimization of enzymes. Besides creating useful catalysts, the generation and iterative improvement of designed enzymes can provide valuable insight into the interplay between the many phenomena that have been suggested to contribute to catalysis. In this work, we follow changes in conformational sampling, electrostatic preorganization, and quantum tunneling along the evolutionary trajectory of a designed Kemp eliminase. We observe that in the Kemp Eliminase KE07, instability of the designed active site leads to the emergence of two additional active site configurations. Evolutionary conformational selection then gradually stabilizes the most efficient configuration, leading to an improved enzyme. This work exemplifies the link between conformational plasticity and evolvability and demonstrates that residues remote from the active sites of enzymes play crucial roles in controlling and shaping the active site for efficient catalysis.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
7001 a Petrovic, Dusanu Uppsala universitet,Biokemi4 aut0 (Swepub:uu)duspe724
7001 a Lee, Richmondu Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia4 aut
7001 a Gryn'ova, Gannau Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia;Ecole Polytech Fed Lausanne, Inst Sci & Ingn Chim, CH-1015 Lausanne, Switzerland4 aut
7001 a Purg, Mihau Uppsala universitet,Biokemi4 aut0 (Swepub:uu)mihpu392
7001 a Saunders, Jakeu Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia4 aut
7001 a Bauer, Paulu Uppsala universitet,Biokemi4 aut0 (Swepub:uu)pauba337
7001 a Carr, Paul D.u Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia4 aut
7001 a Lin, Ching-Yehu Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia4 aut
7001 a Mabbitt, Peter D.u Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia4 aut
7001 a Zhang, Williamu Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia4 aut
7001 a Altamore, Timothyu Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia4 aut
7001 a Easton, Chrisu Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia4 aut
7001 a Coote, Michelle L.u Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia4 aut
7001 a Kamerlin, Shina C. Lynn,d 1981-u Uppsala universitet,Biokemi4 aut0 (Swepub:uu)lynka392
7001 a Jackson, Colin J.u Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australia4 aut
7102 a Australian Natl Univ, Res Sch Chem, Canberra, ACT 2601, Australiab Biokemi4 org
7730 t Nature Communicationsd : Nature Publishing Groupg 9q 9x 2041-1723
8564 u https://doi.org/10.1038/s41467-018-06305-yy Fulltext
8564 u https://uu.diva-portal.org/smash/get/diva2:1256941/FULLTEXT02.pdfx primaryx Raw objecty fulltext:print
8564 u https://www.nature.com/articles/s41467-018-06305-y.pdf
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-363422
8564 8u https://doi.org/10.1038/s41467-018-06305-y

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