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

doi:10.1074/jbc.M113.496778

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

Department of Biological Science and Technology

Research output: Contribution to journal › Article › peer-review

25 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 language	English
Pages (from-to)	30645-30658
Number of pages	14
Journal	Journal of Biological Chemistry
Volume	288
Issue number	42
DOIs	https://doi.org/10.1074/jbc.M113.496778
State	Published - 18 Oct 2013

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Hsieh, Y. C., Chen, M. C., Hsu, C. C., Chan, S. I., Yang, Y.-S., & Chen, C. J. (2013). Crystal structures of vertebrate dihydropyrimidinase and complexes from tetraodon nigroviridis with lysine carbamylation: Metal and structural requirements for post-translational modification and function. Journal of Biological Chemistry, 288(42), 30645-30658. https://doi.org/10.1074/jbc.M113.496778

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

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.",

author = "Hsieh, {Yin Cheng} and Chen, {Mei Chun} and Hsu, {Ching Chen} and Chan, {Sunney I.} and Yuh-Shyong Yang and Chen, {Chun Jung}",

year = "2013",

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doi = "10.1074/jbc.M113.496778",

language = "English",

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Hsieh, YC, Chen, MC, Hsu, CC, Chan, SI, Yang, Y-S & Chen, CJ 2013, 'Crystal structures of vertebrate dihydropyrimidinase and complexes from tetraodon nigroviridis with lysine carbamylation: Metal and structural requirements for post-translational modification and function', Journal of Biological Chemistry, vol. 288, no. 42, pp. 30645-30658. https://doi.org/10.1074/jbc.M113.496778

Crystal structures of vertebrate dihydropyrimidinase and complexes from tetraodon nigroviridis with lysine carbamylation: Metal and structural requirements for post-translational modification and function. / Hsieh, Yin Cheng; Chen, Mei Chun; Hsu, Ching Chen et al.
In: Journal of Biological Chemistry, Vol. 288, No. 42, 18.10.2013, p. 30645-30658.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Crystal structures of vertebrate dihydropyrimidinase and complexes from tetraodon nigroviridis with lysine carbamylation

T2 - Metal and structural requirements for post-translational modification and function

AU - Hsieh, Yin Cheng

AU - Chen, Mei Chun

AU - Hsu, Ching Chen

AU - Chan, Sunney I.

AU - Yang, Yuh-Shyong

AU - Chen, Chun Jung

PY - 2013/10/18

Y1 - 2013/10/18

N2 - 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.

AB - 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.

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DO - 10.1074/jbc.M113.496778

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AN - SCOPUS:84886871577

SN - 0021-9258

VL - 288

SP - 30645

EP - 30658

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 42

ER -

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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