期刊
CELL CHEMICAL BIOLOGY
卷 26, 期 7, 页码 960-+出版社
CELL PRESS
DOI: 10.1016/j.chembiol.2019.03.014
关键词
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资金
- NIH [DK45776]
- NIGMS Training Grant [5 F32 GM113405]
- Life Sciences Institute (University of Michigan)
Allosteric regulation of methylmalonyl-CoA mutase (MCM) by the G-protein chaperone CblA is transduced via three switch elements that gate the movement of the B-12 cofactor to and from MCM. Mutations in CblA and MCM cause hereditary methylmalonic aciduria. Unlike the bacterial orthologs used previously to model disease-causing mutations, human MCM and CblA exhibit a complex pattern of regulation that involves interconverting oligomers, which are differentially sensitive to the presence of GTP versus GDP. Patient mutations in the switch III region of CblA perturb the nucleotide-sensitive distribution of the oligomeric complexes with MCM, leading to loss of regulated movement of B-12 to and/or from MCM and explain the molecular mechanism of the resulting disease.
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