Energetics of Interaction between the G-protein Chaperone, MeaB, and B12-dependent Methylmalonyl-CoA Mutase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference25 articles.
1. Nickel uptake and utilization by microorganisms
2. Classification and evolution of P-loop GTPases and related ATPases
3. Sequence of the Klebsiella aerogenes urease genes and evidence for accessory proteins facilitating nickel incorporation
4. UreG, a Chaperone in the Urease Assembly Process, Is an Intrinsically Unstructured GTPase That Specifically Binds Zn2+
5. HypB protein of Bradyrhizobium japonicum is a metal-binding GTPase capable of binding 18 divalent nickel ions per dimer.
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1. Characterization of a Structurally Distinct ATP-Dependent Reactivating Factor of Adenosylcobalamin-Dependent Lysine 5,6-Aminomutase;Biochemistry;2024-03-12
2. Cobalt–Sulfur Coordination Chemistry Drives B12 Loading onto Methionine Synthase;Journal of the American Chemical Society;2023-11-02
3. Structural insight into G-protein chaperone-mediated maturation of a bacterial adenosylcobalamin-dependent mutase;Journal of Biological Chemistry;2023-09
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5. Architecture of the human G-protein-methylmalonyl-CoA mutase nanoassembly for B12 delivery and repair;Nature Communications;2023-07-19
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