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Crystal structure of the acyl acid amido synthetase GH3-8 from Oryza sativa.
Biochem Biophys Res Commun. 2021 01 01; 534:266-271.BB

Abstract

The Gretchen Hagen 3 (GH3) family of acyl acid amido synthetases regulate the levels and activities of plant hormones containing carboxyl groups, thereby modulating diverse physiological responses. While structure-function relationships have been elucidated for dicotyledonous GH3s, the catalytic mechanism of monocotyledonous GH3 remains elusive. Rice (Oryza sativa) is a representative monocot, and its yield is controlled by the natural growth hormone IAA (indole-3-acetic acid). OsGH3-8 is a model GH3 enzyme that conjugates excess IAA to amino acids in an ATP-dependent manner, ensuring auxin homeostasis and regulating disease resistance, growth and development. Here, we report the crystal structure of OsGH3-8 protein in complex with AMP to uncover the molecular and structural basis for the activity of monocotyledonous GH3-8. Structural and sequence comparisons with other GH3 proteins reveal that the AMP/ATP binding sites are highly conserved. Molecular docking studies with IAA, the GH3-inhibitor Adenosine-5'-[2-(1H-indol-3-yl)ethyl]phosphate (AIEP), and Aspartate provide important information for substrate binding and selectivity of OsGH3-8. Moreover, the observation that AIEP nearly occupies the entire binding site for AMP, IAA and amino acid, offers a ready explanation for the inhibitory effect of AIEP. Taken together, the present study provides vital insights into the molecular mechanisms of monocot GH3 function, and will help to shape the future designs of effective inhibitors.

Authors+Show Affiliations

State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, College of Life Science and Technology, Guangxi Key Laboratory for Sugarcane Biology, Guangxi University, Nanning, 530004, PR China.State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, College of Life Science and Technology, Guangxi Key Laboratory for Sugarcane Biology, Guangxi University, Nanning, 530004, PR China.State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, College of Life Science and Technology, Guangxi Key Laboratory for Sugarcane Biology, Guangxi University, Nanning, 530004, PR China.State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, College of Life Science and Technology, Guangxi Key Laboratory for Sugarcane Biology, Guangxi University, Nanning, 530004, PR China.State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, College of Life Science and Technology, Guangxi Key Laboratory for Sugarcane Biology, Guangxi University, Nanning, 530004, PR China.State Key Laboratory for Conservation and Utilization of Subtropical Agro-bioresources, College of Life Science and Technology, Guangxi Key Laboratory for Sugarcane Biology, Guangxi University, Nanning, 530004, PR China. Electronic address: zhming@gxu.edu.cn.

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

33272567

Citation

Xu, Guolyu, et al. "Crystal Structure of the Acyl Acid Amido Synthetase GH3-8 From Oryza Sativa." Biochemical and Biophysical Research Communications, vol. 534, 2021, pp. 266-271.
Xu G, Zhang Y, Li M, et al. Crystal structure of the acyl acid amido synthetase GH3-8 from Oryza sativa. Biochem Biophys Res Commun. 2021;534:266-271.
Xu, G., Zhang, Y., Li, M., Jiao, X., Zhou, L., & Ming, Z. (2021). Crystal structure of the acyl acid amido synthetase GH3-8 from Oryza sativa. Biochemical and Biophysical Research Communications, 534, 266-271. https://doi.org/10.1016/j.bbrc.2020.11.098
Xu G, et al. Crystal Structure of the Acyl Acid Amido Synthetase GH3-8 From Oryza Sativa. Biochem Biophys Res Commun. 2021 01 1;534:266-271. PubMed PMID: 33272567.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystal structure of the acyl acid amido synthetase GH3-8 from Oryza sativa. AU - Xu,Guolyu, AU - Zhang,Yukun, AU - Li,Mingyang, AU - Jiao,Xi, AU - Zhou,Le, AU - Ming,Zhenhua, Y1 - 2020/12/01/ PY - 2020/11/25/received PY - 2020/11/25/accepted PY - 2020/12/5/pubmed PY - 2020/12/5/medline PY - 2020/12/4/entrez KW - Active site KW - Acyl acid amido synthetases KW - Auxin KW - Protein structure SP - 266 EP - 271 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 534 N2 - The Gretchen Hagen 3 (GH3) family of acyl acid amido synthetases regulate the levels and activities of plant hormones containing carboxyl groups, thereby modulating diverse physiological responses. While structure-function relationships have been elucidated for dicotyledonous GH3s, the catalytic mechanism of monocotyledonous GH3 remains elusive. Rice (Oryza sativa) is a representative monocot, and its yield is controlled by the natural growth hormone IAA (indole-3-acetic acid). OsGH3-8 is a model GH3 enzyme that conjugates excess IAA to amino acids in an ATP-dependent manner, ensuring auxin homeostasis and regulating disease resistance, growth and development. Here, we report the crystal structure of OsGH3-8 protein in complex with AMP to uncover the molecular and structural basis for the activity of monocotyledonous GH3-8. Structural and sequence comparisons with other GH3 proteins reveal that the AMP/ATP binding sites are highly conserved. Molecular docking studies with IAA, the GH3-inhibitor Adenosine-5'-[2-(1H-indol-3-yl)ethyl]phosphate (AIEP), and Aspartate provide important information for substrate binding and selectivity of OsGH3-8. Moreover, the observation that AIEP nearly occupies the entire binding site for AMP, IAA and amino acid, offers a ready explanation for the inhibitory effect of AIEP. Taken together, the present study provides vital insights into the molecular mechanisms of monocot GH3 function, and will help to shape the future designs of effective inhibitors. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/33272567/Crystal_structure_of_the_acyl_acid_amido_synthetase_GH3_8_from_Oryza_sativa_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(20)32142-2 DB - PRIME DP - Unbound Medicine ER -