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| | <StructureSection load='6pk1' size='340' side='right'caption='[[6pk1]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='6pk1' size='340' side='right'caption='[[6pk1]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6pk1]] 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=6PK1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PK1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6pk1]] 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=6PK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PK1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3PY:3-HYDROXYPYRUVIC+ACID'>3PY</scene>, <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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6pk3|6pk3]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PY:3-HYDROXYPYRUVIC+ACID'>3PY</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AGT1, At2g13360, F14O4.7 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=6pk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pk1 OCA], [https://pdbe.org/6pk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pk1 RCSB], [https://www.ebi.ac.uk/pdbsum/6pk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pk1 ProSAT]</span></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=6pk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pk1 OCA], [http://pdbe.org/6pk1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pk1 RCSB], [http://www.ebi.ac.uk/pdbsum/6pk1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pk1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SGAT_ARATH SGAT_ARATH]] Photorespiratory enzyme that catalyzes transamination reactions with multiple substrates, including asparagine. Function exclusively as a catabolic enzyme in Asn metabolism.<ref>PMID:18235971</ref> <ref>PMID:23098902</ref> | + | [https://www.uniprot.org/uniprot/SGAT_ARATH SGAT_ARATH] Photorespiratory enzyme that catalyzes transamination reactions with multiple substrates, including asparagine. Function exclusively as a catabolic enzyme in Asn metabolism.<ref>PMID:18235971</ref> <ref>PMID:23098902</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6pk1" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6pk1" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Aminotransferase 3D structures|Aminotransferase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Liepman, A H]] | + | [[Category: Liepman AH]] |
| - | [[Category: Saper, M A]] | + | [[Category: Saper MA]] |
| - | [[Category: Peroxisomal enzyme]]
| + | |
| - | [[Category: Photorespiration]]
| + | |
| - | [[Category: Plp]]
| + | |
| - | [[Category: Serine-glyoxylate aminotransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
SGAT_ARATH Photorespiratory enzyme that catalyzes transamination reactions with multiple substrates, including asparagine. Function exclusively as a catabolic enzyme in Asn metabolism.[1] [2]
Publication Abstract from PubMed
Photorespiration is an energetically costly metabolic pathway for the recycling of phosphoglycolate produced by the oxygenase activity of ribulose-1,5-bisphosphate carboxylase/oxygenase (RUBISCO) to phosphoglycerate. Arabidopsis alanine:glyoxylate aminotransferase 1 (AGT1) is a peroxisomal aminotransferase with a central role in photorespiration. This enzyme catalyzes various aminotransferase reactions, including serine:glyoxylate, alanine:glyoxylate, and asparagine:glyoxylate transaminations. To better understand structural features that govern the specificity of this enzyme, its crystal structures in the native form (2.2-A resolution) and in the presence of l-serine (2.1-A resolution) were solved. The structures confirm that this enzyme is dimeric, in agreement with studies of the active enzyme in solution. In the crystal, another dimer related by noncrystallographic symmetry makes close interactions to form a tetramer mediated in part by an extra carboxyl-terminal helix conserved in plant homologs of AGT1. Pyridoxal 5'-phosphate (PLP) is bound at the active site but is not held in place by covalent interactions. Residues Tyr35' and Arg36', entering the active site from the other subunits in the dimer, mediate interactions between AGT and l-serine when used as a substrate. In comparison, AGT1 from humans and AGT1 from Anabaena lack these two residues and instead position a tyrosine ring into the binding site, which accounts for their preference for l-alanine instead of l-serine. The structure also rationalizes the phenotype of the sat mutant, Pro251 to Leu, which likely affects the dimer interface near the catalytic site. This structural model of AGT1 provides valuable new information about this protein that may enable improvements to the efficiency of photorespiration.
Crystal Structure Of Photorespiratory Alanine:Glyoxylate Aminotransferase 1 (AGT1) From Arabidopsis thaliana.,Liepman AH, Vijayalakshmi J, Peisach D, Hulsebus B, Olsen LJ, Saper MA Front Plant Sci. 2019 Oct 11;10:1229. doi: 10.3389/fpls.2019.01229. eCollection, 2019. PMID:31681359[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kendziorek M, Paszkowski A. Properties of serine:glyoxylate aminotransferase purified from Arabidopsis thaliana leaves. Acta Biochim Biophys Sin (Shanghai). 2008 Feb;40(2):102-10. doi:, 10.1111/j.1745-7270.2008.00383.x. PMID:18235971 doi:http://dx.doi.org/10.1111/j.1745-7270.2008.00383.x
- ↑ Zhang Q, Lee J, Pandurangan S, Clarke M, Pajak A, Marsolais F. Characterization of Arabidopsis serine:glyoxylate aminotransferase, AGT1, as an asparagine aminotransferase. Phytochemistry. 2013 Jan;85:30-5. doi: 10.1016/j.phytochem.2012.09.017. Epub 2012, Oct 22. PMID:23098902 doi:http://dx.doi.org/10.1016/j.phytochem.2012.09.017
- ↑ Liepman AH, Vijayalakshmi J, Peisach D, Hulsebus B, Olsen LJ, Saper MA. Crystal Structure Of Photorespiratory Alanine:Glyoxylate Aminotransferase 1 (AGT1) From Arabidopsis thaliana. Front Plant Sci. 2019 Oct 11;10:1229. doi: 10.3389/fpls.2019.01229. eCollection, 2019. PMID:31681359 doi:http://dx.doi.org/10.3389/fpls.2019.01229
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