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| | <StructureSection load='5wml' size='340' side='right'caption='[[5wml]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='5wml' size='340' side='right'caption='[[5wml]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wml]] 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=5WML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WML FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wml]] 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=5WML OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WML FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</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]] 2.103Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAT, AAT, MEE17, At2g22250, T26C19.9 ([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=GLU:GLUTAMIC+ACID'>GLU</scene>, <scene name='pdbligand=PMP:4-DEOXY-4-AMINOPYRIDOXAL-5-PHOSPHATE'>PMP</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=5wml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wml OCA], [http://pdbe.org/5wml PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wml RCSB], [http://www.ebi.ac.uk/pdbsum/5wml PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wml ProSAT]</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=5wml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wml OCA], [https://pdbe.org/5wml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wml RCSB], [https://www.ebi.ac.uk/pdbsum/5wml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wml ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PAT_ARATH PAT_ARATH]] Prokaryotic-type aspartate aminotransferase. Has also a prenate transaminase activity. Involved in the aromatic amino acids biosynthesis pathway via the arogenate route. Required for the transamination of prephenate into arogenate. Required for early development of the embryo.<ref>PMID:15634699</ref> <ref>PMID:16623902</ref> <ref>PMID:20883697</ref> | + | [https://www.uniprot.org/uniprot/PAT_ARATH PAT_ARATH] Prokaryotic-type aspartate aminotransferase. Has also a prenate transaminase activity. Involved in the aromatic amino acids biosynthesis pathway via the arogenate route. Required for the transamination of prephenate into arogenate. Required for early development of the embryo.<ref>PMID:15634699</ref> <ref>PMID:16623902</ref> <ref>PMID:20883697</ref> |
| | <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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Holland, C K]] | + | [[Category: Holland CK]] |
| - | [[Category: Jez, J M]] | + | [[Category: Jez JM]] |
| - | [[Category: Aspartate aminotransferase]]
| + | |
| - | [[Category: Plp-dependent]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
PAT_ARATH Prokaryotic-type aspartate aminotransferase. Has also a prenate transaminase activity. Involved in the aromatic amino acids biosynthesis pathway via the arogenate route. Required for the transamination of prephenate into arogenate. Required for early development of the embryo.[1] [2] [3]
Publication Abstract from PubMed
Aromatic amino acids are protein building blocks and precursors to a number of plant natural products, such as the structural polymer lignin and a variety of medicinally relevant compounds. Plants make tyrosine and phenylalanine by a different pathway from many microbes; this pathway requires prephenate aminotransferase (PAT) as the key enzyme. Prephenate aminotransferase produces arogenate, the unique and immediate precursor for both tyrosine and phenylalanine in plants, and also has aspartate aminotransferase (AAT) activity. The molecular mechanisms governing the substrate specificity and activation or inhibition of PAT are currently unknown. Here we present the X-ray crystal structures of the wild-type and various mutants of PAT from Arabidopsis thaliana (AtPAT). Steady-state kinetic and ligand-binding analyses identified key residues, such as Glu108, that are involved in both keto acid and amino acid substrate specificities and probably contributed to the evolution of PAT activity among class Ib AAT enzymes. Structures of AtPAT mutants co-crystallized with either alpha-ketoglutarate or pyridoxamine 5'-phosphate and glutamate further define the molecular mechanisms underlying recognition of keto acid and amino acid substrates. Furthermore, cysteine was identified as an inhibitor of PAT from A. thaliana and Antirrhinum majus plants as well as the bacterium Chlorobium tepidum, uncovering a potential new effector of PAT.
Structural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis.,Holland CK, Berkovich DA, Kohn ML, Maeda H, Jez JM Plant J. 2018 Apr;94(2):304-314. doi: 10.1111/tpj.13856. Epub 2018 Mar 14. PMID:29405514[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Pagnussat GC, Yu HJ, Ngo QA, Rajani S, Mayalagu S, Johnson CS, Capron A, Xie LF, Ye D, Sundaresan V. Genetic and molecular identification of genes required for female gametophyte development and function in Arabidopsis. Development. 2005 Feb;132(3):603-14. Epub 2005 Jan 5. PMID:15634699 doi:http://dx.doi.org/dev.01595
- ↑ de la Torre F, De Santis L, Suarez MF, Crespillo R, Canovas FM. Identification and functional analysis of a prokaryotic-type aspartate aminotransferase: implications for plant amino acid metabolism. Plant J. 2006 May;46(3):414-25. PMID:16623902 doi:http://dx.doi.org/TPJ2713
- ↑ Graindorge M, Giustini C, Jacomin AC, Kraut A, Curien G, Matringe M. Identification of a plant gene encoding glutamate/aspartate-prephenate aminotransferase: the last homeless enzyme of aromatic amino acids biosynthesis. FEBS Lett. 2010 Oct 22;584(20):4357-60. doi: 10.1016/j.febslet.2010.09.037. Epub , 2010 Sep 29. PMID:20883697 doi:http://dx.doi.org/10.1016/j.febslet.2010.09.037
- ↑ Holland CK, Berkovich DA, Kohn ML, Maeda H, Jez JM. Structural basis for substrate recognition and inhibition of prephenate aminotransferase from Arabidopsis. Plant J. 2018 Apr;94(2):304-314. doi: 10.1111/tpj.13856. Epub 2018 Mar 14. PMID:29405514 doi:http://dx.doi.org/10.1111/tpj.13856
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