Document Detail


Crystal structure of an indole-3-acetic acid amido synthetase from grapevine involved in auxin homeostasis.
MedLine Citation:
PMID:  23136372     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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:
Thomas S Peat; Christine Böttcher; Janet Newman; Del Lucent; Nathan Cowieson; Christopher Davies
Publication Detail:
Type:  Journal Article     Date:  2012-11-06
Journal Detail:
Title:  The Plant cell     Volume:  24     ISSN:  1532-298X     ISO Abbreviation:  Plant Cell     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2013-01-01     Completed Date:  2013-08-21     Revised Date:  2013-11-05    
Medline Journal Info:
Nlm Unique ID:  9208688     Medline TA:  Plant Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4525-38     Citation Subset:  IM    
Affiliation:
The Commonwealth Scientific and Industrial Research Organization Materials, Science and Engineering, Parkville, Victoria 3052, Australia.
Data Bank Information
Bank Name/Acc. No.:
PDB/4B2G
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Amino Acids / metabolism
Arabidopsis / chemistry,  enzymology,  genetics
Crystallography, X-Ray
Enzyme Inhibitors
Fruit / chemistry,  enzymology,  genetics
Gene Expression Regulation, Plant
Homeostasis
Indoleacetic Acids / metabolism*
Kinetics
Ligases / antagonists & inhibitors,  chemistry,  genetics
Models, Molecular
Mutagenesis, Site-Directed
Plant Growth Regulators / metabolism*
Plant Proteins / antagonists & inhibitors,  chemistry*,  genetics
Protein Binding
Protein Conformation
Protein Structure, Tertiary
Substrate Specificity
Vitis / chemistry,  enzymology*,  genetics
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Enzyme Inhibitors; 0/Indoleacetic Acids; 0/Plant Growth Regulators; 0/Plant Proteins; 6U1S09C61L/indoleacetic acid; EC 6.-/Ligases
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Development and Validation of Energy Expenditure Prediction Models Based on GT3X Accelerometer Data ...
Next Document:  The novel plant protein INAPERTURATE POLLEN1 marks distinct cellular domains and controls formation ...