ArticleNature chemical biology2013
A switch III motif relays signaling between a B12 enzyme and its G-protein chaperone.
Article in Nature chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed.
- Statistical Analysis of Walker-A Motif-Containing β-α-β Supersecondary Structures in the Protein Data Bank.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Bacterial Metallostasis: Metal Sensing, Metalloproteome Remodeling, and Metal Trafficking.Chemical reviews · 2024Review
- Cobalt-Sulfur Coordination Chemistry Drives BJournal of the American Chemical Society · 2023Article
- Architecture of the human G-protein-methylmalonyl-CoA mutase nanoassembly for BNature communications · 2023Article
- Bivalent molecular mimicry by ADP protects metal redox state and promotes coenzyme BProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structure of metallochaperone in complex with the cobalamin-binding domain of its target mutase provides insight into cofactor delivery.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Very long-term outcomes in 23 patients with cblA type methylmalonic acidemia.Journal of inherited metabolic disease · 2022Article
- The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes.Metallomics : integrated biometal science · 2022Review
- The human BMethods in enzymology · 2022Article
- Redox-Linked Coordination Chemistry Directs Vitamin BAccounts of chemical research · 2021Article
- The requirement for cobalt in vitamin BBiochimica et biophysica acta. Molecular cell research · 2021Review
- Comprehensive classification of ABC ATPases and their functional radiation in nucleoprotein dynamics and biological conflict systems.Nucleic acids research · 2020Review
- Allosteric Regulation of Oligomerization by a BCell chemical biology · 2019Article
- Switch I-dependent allosteric signaling in a G-protein chaperone-BThe Journal of biological chemistry · 2017Article
- Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical BThe Journal of biological chemistry · 2017Article
- The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain That Mediates Holoenzyme Assembly.The Journal of biological chemistry · 2015Article
- Crystal structures of Mycobacterial MeaB and MMAA-like GTPases.Journal of structural and functional genomics · 2015Article
- Visualization of a radical B12 enzyme with its G-protein chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Autoinhibition and signaling by the switch II motif in the G-protein chaperone of a radical B12 enzyme.The Journal of biological chemistry · 2013Article
- G-protein signaling: A switch saves B12 radical status.Nature chemical biology · 2013Article
Corrections and comments
- Commented on by
Authors and funding
4 authors.
Funding
Abstract
Fidelity during cofactor assembly is essential for the proper functioning of metalloenzymes and is ensured by specific chaperones. MeaB, a G-protein chaperone for the coenzyme B12-dependent radical enzyme methylmalonyl-CoA mutase (MCM), uses the energy of GTP binding, hydrolysis or both to regulate cofactor loading into MCM, protect MCM from inactivation and rescue MCM that is inactivated during turnover. Typically, G proteins signal to client proteins using the conformationally mobile switch I and II loops. Crystallographic snapshots of MeaB reported herein reveal a new switch III element that has substantial conformational plasticity. Using alanine-scanning mutagenesis, we demonstrate that the switch III motif is critical for bidirectional signal transmission of the GTPase-activating protein activity of MCM and the chaperone functions of MeaB in the MeaB-MCM complex. Mutations in the switch III loop identified in patients corrupt this interprotein communication and lead to methylmalonic aciduria, an inborn error of metabolism.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.