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| | ==Crystal structure of Indole-3-acetic Acid Methyltransferase== | | ==Crystal structure of Indole-3-acetic Acid Methyltransferase== |
| - | <StructureSection load='3b5i' size='340' side='right' caption='[[3b5i]], [[Resolution|resolution]] 2.75Å' scene=''> | + | <StructureSection load='3b5i' size='340' side='right'caption='[[3b5i]], [[Resolution|resolution]] 2.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3b5i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3B5I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3b5i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B5I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IAMT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b5i OCA], [http://pdbe.org/3b5i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3b5i RCSB], [http://www.ebi.ac.uk/pdbsum/3b5i PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b5i OCA], [https://pdbe.org/3b5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b5i RCSB], [https://www.ebi.ac.uk/pdbsum/3b5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b5i ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/IAMT1_ARATH IAMT1_ARATH]] Catalyzes the methylation of the free carboxyl end of the plant hormone indole-3-acetic acid (IAA). Converts IAA to IAA methyl ester (MeIAA). Regulates IAA activities by IAA methylation. Methylation of IAA plays an important role in regulating plant development and auxin homeostasis. Required for correct leaf pattern formation. MeIAA seems to be an inactive form of IAA.<ref>PMID:12897246</ref> <ref>PMID:16169896</ref> <ref>PMID:17926040</ref> | + | [https://www.uniprot.org/uniprot/IAMT1_ARATH IAMT1_ARATH] Catalyzes the methylation of the free carboxyl end of the plant hormone indole-3-acetic acid (IAA). Converts IAA to IAA methyl ester (MeIAA). Regulates IAA activities by IAA methylation. Methylation of IAA plays an important role in regulating plant development and auxin homeostasis. Required for correct leaf pattern formation. MeIAA seems to be an inactive form of IAA.<ref>PMID:12897246</ref> <ref>PMID:16169896</ref> <ref>PMID:17926040</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/3b5i_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b5/3b5i_consurf.spt"</scriptWhenChecked> |
| | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Ferrer, J L]] | + | [[Category: Large Structures]] |
| - | [[Category: Noel, J P]] | + | [[Category: Ferrer J-L]] |
| - | [[Category: Indole-3-acetic acid]]
| + | [[Category: Noel JP]] |
| - | [[Category: Methyltransferase]] | + | |
| - | [[Category: S-adenosyl-l-methionine]]
| + | |
| - | [[Category: Sabath family]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
IAMT1_ARATH Catalyzes the methylation of the free carboxyl end of the plant hormone indole-3-acetic acid (IAA). Converts IAA to IAA methyl ester (MeIAA). Regulates IAA activities by IAA methylation. Methylation of IAA plays an important role in regulating plant development and auxin homeostasis. Required for correct leaf pattern formation. MeIAA seems to be an inactive form of IAA.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 methylation of IAA's free carboxyl group. The crystal structure of Arabidopsis (Arabidopsis thaliana) IAMT (AtIAMT1) was determined and refined to 2.75 A resolution. The overall tertiary and quaternary structures closely resemble the two-domain bilobed monomer and the dimeric arrangement, respectively, previously observed for the related salicylic acid 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 one-half of the OsSABATH genes were transcribed in one or multiple organs. The OsSABATH gene most similar to AtIAMT1 is OsSABATH4. Escherichia coli-expressed OsSABATH4 protein displayed the highest level of catalytic activity toward 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 (Populus spp.) 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.
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. 2008 Feb;146(2):455-67. Epub 2007 Dec 27. PMID:18162595[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zubieta C, Ross JR, Koscheski P, Yang Y, Pichersky E, Noel JP. Structural basis for substrate recognition in the salicylic acid carboxyl methyltransferase family. Plant Cell. 2003 Aug;15(8):1704-16. PMID:12897246
- ↑ Qin G, Gu H, Zhao Y, Ma Z, Shi G, Yang Y, Pichersky E, Chen H, Liu M, Chen Z, Qu LJ. An indole-3-acetic acid carboxyl methyltransferase regulates Arabidopsis leaf development. Plant Cell. 2005 Oct;17(10):2693-704. Epub 2005 Sep 16. PMID:16169896 doi:http://dx.doi.org/10.1105/tpc.105.034959
- ↑ Li L, Hou X, Tsuge T, Ding M, Aoyama T, Oka A, Gu H, Zhao Y, Qu LJ. The possible action mechanisms of indole-3-acetic acid methyl ester in Arabidopsis. Plant Cell Rep. 2008 Mar;27(3):575-84. Epub 2007 Oct 10. PMID:17926040 doi:http://dx.doi.org/10.1007/s00299-007-0458-9
- ↑ Zhao N, Ferrer JL, Ross J, Guan J, Yang Y, Pichersky E, Noel JP, Chen F. Structural, biochemical, and phylogenetic analyses suggest that indole-3-acetic acid methyltransferase is an evolutionarily ancient member of the SABATH family. Plant Physiol. 2008 Feb;146(2):455-67. Epub 2007 Dec 27. PMID:18162595 doi:10.1104/pp.107.110049
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