Neutron Crystal Structure of RAS GTPase Puts in Question the Protonation State of the GTP γ-Phosphate

Ryan Knihtila, Genevieve Holzapfel, Kevin Weiss, Flora Meilleur, Carla Mattos

Research output: Contribution to journalArticlepeer-review

39 Scopus citations

Abstract

Background: The GTP nucleotide is thought to be fully deprotonated when bound to RAS. Results: The neutron crystal structure of RAS bound to the GTP analogue GppNHp shows a protonated γ-phosphate. Conclusion: The active site of RAS significantly increases the pKa of the nucleotide. Significance: This work provides insight to the GTP hydrolysis mechanism, with implications to the superfamily of small GTPases.

Original languageEnglish
Pages (from-to)31025-31036
Number of pages12
JournalJournal of Biological Chemistry
Volume290
Issue number52
DOIs
StatePublished - Dec 25 2015

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