ArticleThe Journal of biological chemistry2015
Neutron Crystal Structure of RAS GTPase Puts in Question the Protonation State of the GTP γ-Phosphate.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 43 citations in OpenAlex.
- Far-reaching effects of tyrosine64 phosphorylation on Ras revealed with BeFCommunications chemistry · 2024Article
- Allosteric site variants affect GTP hydrolysis on Ras.Protein science : a publication of the Protein Society · 2023Article
- Mechanisms of isoform-specific residue influence on GTP-bound HRas, KRas, and NRas.Biophysical journal · 2022Article
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
- Article
- Novel MAPK/AKT-impairing germline NRAS variant identified in a melanoma-prone family.Familial cancer · 2022Article
- The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and x-ray diffraction at room temperature.Science advances · 2022Article
- The mechanisms of catalysis and ligand binding for the SARS-CoV-2 NSP3 macrodomain from neutron and X-ray diffraction at room temperature.bioRxiv : the preprint server for biology · 2022Article
- Crystal Structure Reveals the Full Ras-Raf Interface and Advances Mechanistic Understanding of Raf Activation.Biomolecules · 2021Article
- Identification of LRRK2 missense variants in the accelerating medicines partnership Parkinson's disease cohort.Human molecular genetics · 2021Article
- Article
- A H-REV107 Peptide Inhibits Tumor Growth and Interacts Directly with Oncogenic KRAS Mutants.Cancers · 2020Article
- Recent Advances in Understanding Biological GTP Hydrolysis through Molecular Simulation.ACS omega · 2020Review
- Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix.Acta crystallographica. Section D, Structural biology · 2019Article
- Isoform-Specific Destabilization of the Active Site Reveals a Molecular Mechanism of Intrinsic Activation of KRas G13D.Cell reports · 2019Article
- Titration of ionizable groups in proteins using multiple neutron data sets from a single crystal: application to the small GTPase Ras.Acta crystallographica. Section F, Structural biology communications · 2019Article
- The Ras Superfamily of Small GTPases in Non-neoplastic Cerebral Diseases.Frontiers in molecular neuroscience · 2019Review
- Neutron and X-ray crystal structures of Lactobacillus brevis alcohol dehydrogenase reveal new insights into hydrogen-bonding pathways.Acta crystallographica. Section F, Structural biology communications · 2018Article
- The bacterial Ras/Rap1 site-specific endopeptidase RRSP cleaves Ras through an atypical mechanism to disrupt Ras-ERK signaling.Science signaling · 2018Article
- The K-Ras, N-Ras, and H-Ras Isoforms: Unique Conformational Preferences and Implications for Targeting Oncogenic Mutants.Cold Spring Harbor perspectives in medicine · 2018Review
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RAS GTPase is a prototype for nucleotide-binding proteins that function by cycling between GTP and GDP, with hydrogen atoms playing an important role in the GTP hydrolysis mechanism. It is one of the most well studied proteins in the superfamily of small GTPases, which has representatives in a wide range of cellular functions. These proteins share a GTP-binding pocket with highly conserved motifs that promote hydrolysis to GDP. The neutron crystal structure of RAS presented here strongly supports a protonated γ-phosphate at physiological pH. This counters the notion that the phosphate groups of GTP are fully deprotonated at the start of the hydrolysis reaction, which has colored the interpretation of experimental and computational data in studies of the hydrolysis mechanism. The neutron crystal structure presented here puts in question our understanding of the pre-catalytic state associated with the hydrolysis reaction central to the function of RAS and other GTPases.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.