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Crystal structure of an indole-3-acetic acid amido synthetase from grapevine involved in auxin homeostasis.
Plant Cell. 2012 Nov; 24(11):4525-38.PC

Abstract

Auxins are important for plant growth and development, including the control of fruit ripening. Conjugation to amino acids by indole-3-acetic acid (IAA)-amido synthetases is an important part of auxin homeostasis. The structure of the auxin-conjugating Gretchen Hagen3-1 (GH3-1) enzyme from grapevine (Vitis vinifera), in complex with an inhibitor (adenosine-5'-[2-(1H-indol-3-yl)ethyl]phosphate), is presented. Comparison with a previously published benzoate-conjugating enzyme from Arabidopsis thaliana indicates that grapevine GH3-1 has a highly similar domain structure and also undergoes a large conformational change during catalysis. Mutational analyses and structural comparisons with other proteins have identified residues likely to be involved in acyl group, amino acid, and ATP substrate binding. Vv GH3-1 is a monomer in solution and requires magnesium ions solely for the adenlyation reaction. Modeling of IAA and two synthetic auxins, benzothiazole-2-oxyacetic acid (BTOA) and 1-naphthaleneacetic acid (NAA), into the active site indicates that NAA and BTOA are likely to be poor substrates for this enzyme, confirming previous enzyme kinetic studies. This suggests a reason for the increased effectiveness of NAA and BTOA as auxins in planta and provides a tool for designing new and effective auxins.

Authors+Show Affiliations

The Commonwealth Scientific and Industrial Research Organization Materials, Science and Engineering, Parkville, Victoria 3052, Australia.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

23136372

Citation

Peat, Thomas S., et al. "Crystal Structure of an Indole-3-acetic Acid Amido Synthetase From Grapevine Involved in Auxin Homeostasis." The Plant Cell, vol. 24, no. 11, 2012, pp. 4525-38.
Peat TS, Böttcher C, Newman J, et al. Crystal structure of an indole-3-acetic acid amido synthetase from grapevine involved in auxin homeostasis. Plant Cell. 2012;24(11):4525-38.
Peat, T. S., Böttcher, C., Newman, J., Lucent, D., Cowieson, N., & Davies, C. (2012). Crystal structure of an indole-3-acetic acid amido synthetase from grapevine involved in auxin homeostasis. The Plant Cell, 24(11), 4525-38. https://doi.org/10.1105/tpc.112.102921
Peat TS, et al. Crystal Structure of an Indole-3-acetic Acid Amido Synthetase From Grapevine Involved in Auxin Homeostasis. Plant Cell. 2012;24(11):4525-38. PubMed PMID: 23136372.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystal structure of an indole-3-acetic acid amido synthetase from grapevine involved in auxin homeostasis. AU - Peat,Thomas S, AU - Böttcher,Christine, AU - Newman,Janet, AU - Lucent,Del, AU - Cowieson,Nathan, AU - Davies,Christopher, Y1 - 2012/11/06/ PY - 2012/11/9/entrez PY - 2012/11/9/pubmed PY - 2013/8/22/medline SP - 4525 EP - 38 JF - The Plant cell JO - Plant Cell VL - 24 IS - 11 N2 - Auxins are important for plant growth and development, including the control of fruit ripening. Conjugation to amino acids by indole-3-acetic acid (IAA)-amido synthetases is an important part of auxin homeostasis. The structure of the auxin-conjugating Gretchen Hagen3-1 (GH3-1) enzyme from grapevine (Vitis vinifera), in complex with an inhibitor (adenosine-5'-[2-(1H-indol-3-yl)ethyl]phosphate), is presented. Comparison with a previously published benzoate-conjugating enzyme from Arabidopsis thaliana indicates that grapevine GH3-1 has a highly similar domain structure and also undergoes a large conformational change during catalysis. Mutational analyses and structural comparisons with other proteins have identified residues likely to be involved in acyl group, amino acid, and ATP substrate binding. Vv GH3-1 is a monomer in solution and requires magnesium ions solely for the adenlyation reaction. Modeling of IAA and two synthetic auxins, benzothiazole-2-oxyacetic acid (BTOA) and 1-naphthaleneacetic acid (NAA), into the active site indicates that NAA and BTOA are likely to be poor substrates for this enzyme, confirming previous enzyme kinetic studies. This suggests a reason for the increased effectiveness of NAA and BTOA as auxins in planta and provides a tool for designing new and effective auxins. SN - 1532-298X UR - https://www.unboundmedicine.com/medline/citation/23136372/Crystal_structure_of_an_indole_3_acetic_acid_amido_synthetase_from_grapevine_involved_in_auxin_homeostasis_ L2 - https://academic.oup.com/plcell/article-lookup/doi/10.1105/tpc.112.102921 DB - PRIME DP - Unbound Medicine ER -