3b5i
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(New page: 200px<br /><applet load="3b5i" size="350" color="white" frame="true" align="right" spinBox="true" caption="3b5i, resolution 2.75Å" /> '''Crystal structure of...)
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Revision as of 09:11, 23 January 2008
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Crystal structure of Indole-3-acetic Acid Methyltransferase
Overview
The plant SABATH protein family encompasses a group of related small, molecule methyltransferases (MTs) that catalyze the, S-adenosyl-L-methionine dependent methylation of natural chemicals, encompassing widely divergent structures. Indole-3-acetic acid (IAA), methyltransferase (IAMT) is a member of the SABATH family that modulates, IAA homeostasis in plant tissues through the methylation of IAA's free, carboxyl group. The crystal structure of Arabidopsis thaliana IAMT, (AtIAMT1) was determined and refined to 2.75 A resolution. The overall, tertiary and quaternary structures closely resemble the two-domain, bi-lobed monomer and the dimeric arrangement, respectively, previously, observed for the related salicylic acid (SA) carboxyl methyltransferase, from Clarkia breweri (CbSAMT). To further our understanding of the, biological function and evolution of SABATHs, especially of IAMT, we, analyzed the SABATH gene family in the rice (Oryza sativa) genome. Forty, one OsSABATH genes were identified. Expression analysis showed that more, than half of the OsSABATH genes were transcribed in one or multiple, organs. The OsSABATH gene most similar to AtIAMT1 is OsSABATH4. E., coli-expressed OsSABATH4 protein displayed the highest level of catalytic, activity towards IAA, and was therefore named OsIAMT1. OsIAMT1 exhibited, kinetic properties similar to AtIAMT1 and poplar IAMT (PtIAMT1)., Structural modeling of OsIAMT1 and PtIAMT1 using the experimentally, determined structure of AtIAMT1 reported here as a template revealed, conserved structural features of IAMTs within the active site cavity that, are divergent from functionally distinct members of the SABATH family such, as CbSAMT. Phylogenetic analysis revealed that IAMTs from Arabidopsis, rice and poplar form a monophyletic group. Thus, structural, biochemical, and phylogenetic evidence supports the hypothesis that IAMT is an, evolutionarily ancient member of the SABATH family likely to play a, critical role in IAA homeostasis across a wide range of plants.
About this Structure
3B5I is a Single protein structure of sequence from Arabidopsis thaliana with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural, Biochemical and Phylogenetic Analyses Suggest that Indole-3-acetic Acid Methyltransferase Is An Evolutionarily Ancient Member of the SABATH Family., Zhao N, Ferrer JL, Ross J, Guan J, Yang Y, Pichersky E, Noel JP, Chen F, Plant Physiol. 2007 Dec 27;. PMID:18162595
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