Insights into open/closed conformations of the catalytically active human guanylate kinase as investigated by small-angle X-ray scattering
2016-01-01 | journal article. A publication with affiliation to the University of Göttingen.
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Insights into open/closed conformations of the catalytically active human guanylate kinase as investigated by small-angle X-ray scattering
Jain, R.; Khan, N.; Menzel, A.; Rajkovic, I.; Konrad, M. & Techert, S. (2016)
European Biophysics Journal, 45(1) pp. 81-89. DOI: https://doi.org/10.1007/s00249-015-1079-9
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- Authors
- Jain, Rohit; Khan, Nazimuddin; Menzel, Andreas; Rajkovic, Ivan; Konrad, Manfred; Techert, Simone
- Abstract
- Bio-catalysis is the outcome of a subtle interplay between internal motions in enzymes and chemical kinetics. Small-angle X-ray scattering (SAXS) investigation of an enzyme's internal motions during catalysis offers an integral view of the protein's structural plasticity, dynamics, and function, which is useful for understanding allosteric effects and developing novel medicines. Guanylate kinase (GMPK) is an essential enzyme involved in the guanine nucleotide metabolism of unicellular and multicellular organisms. It is also required for the intracellular activation of numerous antiviral and anticancer purine nucleoside analog prodrugs. Catalytically active recombinant human GMPK (hGMPK) was purified for the first time and changes in the size and shape of open/closed hGMPK were tracked by SAXS. The binding of substrates (GMP + AMPPNP or Ap5G or GMP + ADP) resulted in the compaction of size and shape of hGMPK. The structural changes between open and completely closed hGMPK conformation were confirmed by observing differences in the hGMPK secondary structures with circular dichroism spectroscopy. [GRAPHICS]
- Issue Date
- 1-January-2016
- Journal
- European Biophysics Journal
- Organization
- Fakultät für Physik ; Institut für Röntgenphysik
- Working Group
- RG Techert (Structural Dynamics in Chemical Systems)
- ISSN
- 1432-1017; 0175-7571
- Sponsor
- Max Planck Society; DAAD scholarship; project B10 [SFB 755]