Glycogen phosphorylase revisited: extending the resolution of the R- and T-state structures of the free enzyme and in complex with allosteric activators

Leonidas, D.D.; Zographos, S.E.; Tsitsanou, K.E.; Skamnaki, V.T.; Stravodimos, G.; Kyriakis, E.

doi:10.1107/S2053230X21008542

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 4
Superimposed structures of R-state rmGPb–AMP from co-crystallization (cyan), the structure from a soaking experiment (grey; PDB entry 7gpb) and that of the R-state PLPP enzyme (orange) at the allosteric binding site. Overall structures showing the AMP loop (a) and the residues interacting with AMP in stereo (b).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 77| Part 9| September 2021| Pages 303-311

https://doi.org/10.1107/S2053230X21008542

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