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Crystal structures of vertebrate dihydropyrimidinase and complexes from tetraodon nigroviridis with lysine carbamylation: Metal and structural requirements for post-translational modification and function
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Crystal structures of vertebrate dihydropyrimidinase and complexes from tetraodon nigroviridis with lysine carbamylation: Metal and structural requirements for post-translational modification and function

Yin-Cheng Hsieh, Mei-Chun Chen, Ching-Chen Hsu, Sunney I. Chan, Yuh-Shyong YangChun-Jung Chen
Journal of Biological Chemistry, 卷.288(42), 頁碼.30645-30658
10/2013
PMID: 24005677

摘要

Biochemistry Molecular Biology Cell Biology
Background: Lysine carbamylation facilitates metal coordination for enzymatic activities. Results: Structures of dihydropyrimidinase as the apo and holoenzyme with one and two metals and its substrate/product complexes are determined. Conclusion: The structures reveal four steps in the assembly of the holoprotein with the carbamylated lysine and two metal ions. Significance: The results illustrate how proteins exploit lysines and metals to accomplish lysine carbamylation and enzymatic functions. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

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