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| | ==Crystal structure of Arabidopsis thaliana fatty-acid binding protein At1g53520 (AtFAP3)== | | ==Crystal structure of Arabidopsis thaliana fatty-acid binding protein At1g53520 (AtFAP3)== |
| - | <StructureSection load='4dol' size='340' side='right' caption='[[4dol]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='4dol' size='340' side='right'caption='[[4dol]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dol]] is a 1 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=4DOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DOL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dol]] is a 1 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=4DOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DOL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4doi|4doi]], [[4dok|4dok]], [[4doo|4doo]]</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=4dol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dol OCA], [https://pdbe.org/4dol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dol RCSB], [https://www.ebi.ac.uk/pdbsum/4dol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dol ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At1g53520, F22G10.11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=4dol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dol OCA], [http://pdbe.org/4dol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dol RCSB], [http://www.ebi.ac.uk/pdbsum/4dol PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dol ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FAP3_ARATH FAP3_ARATH]] Fatty-acid-binding protein. Interacts with most fatty acids tested and has maximal relative affinity for C16:0. | + | [[https://www.uniprot.org/uniprot/FAP3_ARATH FAP3_ARATH]] Fatty-acid-binding protein. Interacts with most fatty acids tested and has maximal relative affinity for C16:0. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| - | [[Category: Bowman, M E]] | + | [[Category: Large Structures]] |
| - | [[Category: Louie, G V]] | + | [[Category: Bowman ME]] |
| - | [[Category: Noel, J P]] | + | [[Category: Louie GV]] |
| - | [[Category: Chalcone-isomerase like fold]] | + | [[Category: Noel JP]] |
| - | [[Category: Fatty-acid binding]]
| + | |
| - | [[Category: Isomerase]]
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| Structural highlights
Function
[FAP3_ARATH] Fatty-acid-binding protein. Interacts with most fatty acids tested and has maximal relative affinity for C16:0.
Publication Abstract from PubMed
Specialized metabolic enzymes biosynthesize chemicals of ecological importance, often sharing a pedigree with primary metabolic enzymes. However, the lineage of the enzyme chalcone isomerase (CHI) remained unknown. In vascular plants, CHI-catalysed conversion of chalcones to chiral (S)-flavanones is a committed step in the production of plant flavonoids, compounds that contribute to attraction, defence and development. CHI operates near the diffusion limit with stereospecific control. Although associated primarily with plants, the CHI fold occurs in several other eukaryotic lineages and in some bacteria. Here we report crystal structures, ligand-binding properties and in vivo functional characterization of a non-catalytic CHI-fold family from plants. Arabidopsis thaliana contains five actively transcribed genes encoding CHI-fold proteins, three of which additionally encode amino-terminal chloroplast-transit sequences. These three CHI-fold proteins localize to plastids, the site of de novo fatty-acid biosynthesis in plant cells. Furthermore, their expression profiles correlate with those of core fatty-acid biosynthetic enzymes, with maximal expression occurring in seeds and coinciding with increased fatty-acid storage in the developing embryo. In vitro, these proteins are fatty-acid-binding proteins (FAPs). FAP knockout A. thaliana plants show elevated alpha-linolenic acid levels and marked reproductive defects, including aberrant seed formation. Notably, the FAP discovery defines the adaptive evolution of a stereospecific and catalytically 'perfected' enzyme from a non-enzymatic ancestor over a defined period of plant evolution.
Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis.,Ngaki MN, Louie GV, Philippe RN, Manning G, Pojer F, Bowman ME, Li L, Larsen E, Wurtele ES, Noel JP Nature. 2012 May 13;485(7399):530-3. doi: 10.1038/nature11009. PMID:22622584[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ngaki MN, Louie GV, Philippe RN, Manning G, Pojer F, Bowman ME, Li L, Larsen E, Wurtele ES, Noel JP. Evolution of the chalcone-isomerase fold from fatty-acid binding to stereospecific catalysis. Nature. 2012 May 13;485(7399):530-3. doi: 10.1038/nature11009. PMID:22622584 doi:10.1038/nature11009
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