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Sökning: onr:"swepub:oai:DiVA.org:umu-106747" > Structural basis fo...
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 03041naa a2200421 4500 | |
| 001 | oai:DiVA.org:umu-106747 | |
| 003 | SwePub | |
| 008 | 150806s2015 | |||||||||||000 ||eng| | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-1067472 URI |
| 024 | 7 | a https://doi.org/10.1038/ncomms86442 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 Kovermann, Michaelu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)miko0009 |
| 245 | 1 0 | a Structural basis for catalytically restrictive dynamics of a high-energy enzyme state |
| 264 | c 2015-07-03 | |
| 264 | 1 | b Macmillan Publishers Ltd.c 2015 |
| 338 | a electronic2 rdacarrier | |
| 520 | a An emerging paradigm in enzymology is that transient high-energy structural states play crucial roles in enzymatic reaction cycles. Generally, these high-energy or ‘invisible’ states cannot be studied directly at atomic resolution using existing structural and spectroscopic techniques owing to their low populations or short residence times. Here we report the direct NMR-based detection of the molecular topology and conformational dynamics of a catalytically indispensable high-energy state of an adenylate kinase variant. On the basis of matching energy barriers for conformational dynamics and catalytic turnover, it was found that the enzyme’s catalytic activity is governed by its dynamic interconversion between the high-energy state and a ground state structure that was determined by X-ray crystallography. Our results show that it is possible to rationally tune enzymes’ conformational dynamics and hence their catalytic power—a key aspect in rational design of enzymes catalysing novel reactions. | |
| 650 | 7 | a NATURVETENSKAPx Kemi0 (SwePub)1042 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Chemical Sciences0 (SwePub)1042 hsv//eng |
| 653 | a Biological sciences | |
| 653 | a Biophysics | |
| 653 | a Biochemistry | |
| 700 | 1 | a Ådén, Jörgenu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)jonadn02 |
| 700 | 1 | a Grundström, Christinu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)chgr0001 |
| 700 | 1 | a Sauer-Eriksson, A. Elisabethu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)elsa0002 |
| 700 | 1 | a Sauer, Uwe Hu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)uwsa0001 |
| 700 | 1 | a Wolf-Watz, Magnusu Umeå universitet,Kemiska institutionen4 aut0 (Swepub:umu)maswoz04 |
| 710 | 2 | a Umeå universitetb Kemiska institutionen4 org |
| 773 | 0 | t Nature Communicationsd : Macmillan Publishers Ltd.g 6q 6x 2041-1723 |
| 856 | 4 | u https://doi.org/10.1038/ncomms8644y Fulltext |
| 856 | 4 | u https://umu.diva-portal.org/smash/get/diva2:844540/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print |
| 856 | 4 | u https://www.nature.com/articles/ncomms8644.pdf |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-106747 |
| 856 | 4 8 | u https://doi.org/10.1038/ncomms8644 |
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