globalchange  > 气候变化与战略
DOI: 10.1073/pnas.1908718116
论文题名:
SDS22 selectively recognizes and traps metal-deficient inactive PP1
作者: Choy M.S.; Moon T.M.; Ravindran R.; Bray J.A.; Robinson L.C.; Archuleta T.L.; Shi W.; Peti W.; Tatchell K.; Page R.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2019
卷: 116, 期:41
起始页码: 20472
结束页码: 20481
语种: 英语
英文关键词: Crystal structure ; Inhibitor ; Metal binding ; Protein phosphatase 1 (PP1) ; SDS22
Scopus关键词: cell protein ; phosphoprotein phosphatase 1 ; SDS22 protein ; unclassified drug ; Article ; binding affinity ; binding site ; biogenesis ; biophysics ; catalysis ; controlled study ; crystallography ; enzyme regulation ; enzyme specificity ; immunoblotting ; in vivo study ; nonhuman ; polyacrylamide gel electrophoresis ; priority journal ; protein aggregation ; protein conformation ; protein expression ; protein interaction
英文摘要: The metalloenzyme protein phosphatase 1 (PP1), which is responsible for ≥50% of all dephosphorylation reactions, is regulated by scores of regulatory proteins, including the highly conserved SDS22 protein. SDS22 has numerous diverse functions, surprisingly acting as both a PP1 inhibitor and as an activator. Here, we integrate cellular, biophysical, and crystallographic studies to address this conundrum. We discovered that SDS22 selectively binds a unique conformation of PP1 that contains a single metal (M2) at its active site, i.e., SDS22 traps metal-deficient inactive PP1. Furthermore, we showed that SDS22 dissociation is accompanied by a second metal (M1) being loaded into PP1, as free metal cannot dissociate the complex and M1-deficient mutants remain constitutively trapped by SDS22. Together, our findings reveal that M1 metal loading and loss are essential for PP1 regulation in cells, which has broad implications for PP1 maturation, activity, and holoenzyme subunit exchange. © 2019 National Academy of Sciences. All rights reserved.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163601
Appears in Collections:气候变化与战略

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作者单位: Choy, M.S., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States; Moon, T.M., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States; Ravindran, R., Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, United States; Bray, J.A., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States; Robinson, L.C., Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, United States; Archuleta, T.L., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States; Shi, W., Department of Energy and Photon Sciences, Brookhaven National Laboratory, Upton, NY 11973, United States; Peti, W., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States; Tatchell, K., Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, LA 71130, United States; Page, R., Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ 85721, United States

Recommended Citation:
Choy M.S.,Moon T.M.,Ravindran R.,et al. SDS22 selectively recognizes and traps metal-deficient inactive PP1[J]. Proceedings of the National Academy of Sciences of the United States of America,2019-01-01,116(41)
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