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==Arabidopsis thaliana prephenate aminotransferase== | ==Arabidopsis thaliana prephenate aminotransferase== | ||
<StructureSection load='5wmh' size='340' side='right' caption='[[5wmh]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='5wmh' size='340' side='right'caption='[[5wmh]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5wmh]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WMH OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5wmh]] is a 6 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=5WMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WMH FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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]] 3Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=5wmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wmh OCA], [https://pdbe.org/5wmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wmh RCSB], [https://www.ebi.ac.uk/pdbsum/5wmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wmh ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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;"> | |||
== 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<ref>PMID:29405514</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5wmh" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Arabidopsis thaliana]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Holland CK]] | ||
[[Category: | [[Category: Jez JM]] | ||
Latest revision as of 17:17, 4 October 2023
Arabidopsis thaliana prephenate aminotransferaseArabidopsis thaliana prephenate aminotransferase
Structural highlights
FunctionPAT_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 PubMedAromatic 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 AlsoReferences
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