A Switch III Motif Relays Signaling between a B12 Enzyme and its G-protein Chaperone
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Summary
Using alanine-scanning mutagenesis, it is demonstrated 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.
- Type
- article
- Published
- 2013-07-21
- Cited by
- 30
- References
- 45
- Access
- Open access
- OpenAlex
- https://openalex.org/W23873214
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:16946498
Keywords
Virtualization, Computer science, Operating system, Cloud computing
References
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- Mechanism of reactivation of coenzyme B12-dependent diol dehydratase by a molecular chaperone-like reactivating factor.
- Loss of Allostery and Coenzyme B12 Delivery by a Pathogenic Mutation in Adenosyltransferase
- Activation of methionine synthase: further characterization of flavoprotein system.
- Adenosyltransferase: an enzyme and an escort for coenzyme B12?
- The CCP4 suite: programs for protein crystallography.
- High resolution melting analysis of the MMAA gene in patients with cblA and in those with undiagnosed methylmalonic aciduria.
- Molecular cloning of L-methylmalonyl-CoA mutase: gene transfer and analysis of mut cell lines.
- GNAS1 mutational analysis in pseudohypoparathyroidism
- Characterization, Sequencing, and Expression of the Genes Encoding a Reactivating Factor for Glycerol-inactivated Adenosylcobalamin-dependent Diol Dehydratase*
- Assembly and protection of the radical enzyme, methylmalonyl-CoA mutase, by its chaperone.
- Redox-dependent complex formation by an ATP-dependent activator of the corrinoid/iron-sulfur protein
- Adenosyltransferase tailors and delivers coenzyme B12.
- MeaB Is a Component of the Methylmalonyl-CoA Mutase Complex Required for Protection of the Enzyme from Inactivation*
- A rotary mechanism for coenzyme B(12) synthesis by adenosyltransferase.
- Release of a damaged cofactor from a coenzyme B12-dependent enzyme: X-ray structures of diol dehydratase-reactivating factor.
- Refinement of macromolecular structures by the maximum-likelihood method.
- A G-protein editor gates coenzyme B12 loading and is corrupted in methylmalonic aciduria
- Human Methionine Synthase Reductase, a Soluble P-450 Reductase-like Dual Flavoprotein, Is Sufficient for NADPH-dependent Methionine Synthase Activation*
Cited by
- Crystal structures of Mycobacterial MeaB and MMAA-like GTPases
- Cobalamin-dependent dehydratases and a deaminase: radical catalysis and reactivating chaperones.
- Autoinhibition and Signaling by the Switch II Motif in the G-protein Chaperone of a Radical B12 Enzyme*
- Visualization of a radical B12 enzyme with its G-protein chaperone
- The N-terminal Domain of Escherichia coli Assimilatory NADPH-Sulfite Reductase Hemoprotein Is an Oligomerization Domain That Mediates Holoenzyme Assembly*
- Carbon nitride nanosheet-supported porphyrin: a new biomimetic catalyst for highly efficient bioanalysis.
- Essential roles of nucleotide-switch and metal-coordinating residues for chaperone function of diol dehydratase-reactivase.
- Cofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B12 Enzyme IcmF*♦
- Protein destabilization and loss of protein‐protein interaction are fundamental mechanisms in cblA‐type methylmalonic aciduria
- Visualization of a radical B[subscript 12] enzyme with its G-protein chaperone
- Switch I-dependent allosteric signaling in a G-protein chaperone–B12 enzyme complex
- Allosteric regulation of oligomerization by a B12 trafficking G-protein is corrupted in methylmalonic aciduria
- Crystallographic Snapshots of Functional Motions in Cobalamin Maintenance and Methylphosphonate Production
- Comprehensive classification of ABC ATPases and their functional radiation in nucleoprotein dynamics and biological conflict systems.
- The requirement for cobalt in vitamin B12: A paradigm for protein metalation
- Redox-linked Coordination Chemistry Directs Vitamin B12 Trafficking
- The human B12 trafficking chaperones: CblA, ATR, CblC and CblD
- The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes
- Very long‐term outcomes in 23 patients with cblA type methylmalonic acidemia
- The complex machinery of human cobalamin metabolism
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