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 Yang, Chun Jung Chen*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)30645-30658
Number of pages14
JournalJournal of Biological Chemistry
Volume288
Issue number42
DOIs
StatePublished - 18 Oct 2013

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