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Journal Article

Insights into open/closed conformations of the catalytically active human guanylate kinase as investigated by small-angle X-ray scattering.

MPS-Authors
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Jain,  R.
Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for Biophysical Chemistry, Max Planck Society;

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Rajkovic,  I.
Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for Biophysical Chemistry, Max Planck Society;

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Konrad,  M.
Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society;

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Techert,  S.
Research Group of Structural Dynamics of (Bio)Chemical Systems, MPI for Biophysical Chemistry, Max Planck Society;

External Resource

http://link.springer.com/content/pdf/10.1007%2Fs00249-015-1079-9.pdf
(Publisher version)

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Fulltext (public)

2218438.pdf
(Publisher version), 2MB

Supplementary Material (public)

2218438_Suppl.docx
(Supplementary material), 2MB

Citation

Jain, R., Khan, N., Menzel, A., Rajkovic, I., Konrad, M., & Techert, S. (2016). Insights into open/closed conformations of the catalytically active human guanylate kinase as investigated by small-angle X-ray scattering. European Biophysics Journal, 45(1), 81-89. doi:10.1007/s00249-015-1079-9.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-9771-F
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.