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| <StructureSection load='3vc3' size='340' side='right'caption='[[3vc3]], [[Resolution|resolution]] 1.77Å' scene=''> | | <StructureSection load='3vc3' size='340' side='right'caption='[[3vc3]], [[Resolution|resolution]] 1.77Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[3vc3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VC3 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[3vc3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VC3 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C6P:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-L-CYSTEINE'>C6P</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]] 1.766Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vbe|3vbe]]</div></td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C6P:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-L-CYSTEINE'>C6P</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GLYMA09G39390, OAS-TL3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3847 Glycine hispida])</td></tr> | |
| <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cysteine_synthase Cysteine synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.47 2.5.1.47] </span></td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vc3 OCA], [https://pdbe.org/3vc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vc3 RCSB], [https://www.ebi.ac.uk/pdbsum/3vc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vc3 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=3vc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vc3 OCA], [https://pdbe.org/3vc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vc3 RCSB], [https://www.ebi.ac.uk/pdbsum/3vc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vc3 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/I1L6I6_SOYBN I1L6I6_SOYBN] |
| Plants produce cyanide (CN(-)) during ethylene biosynthesis in the mitochondria and require beta-cyanoalanine synthase (CAS) for CN(-) detoxification. Recent studies show that CAS is a member of the beta-substituted alanine synthase (BSAS) family, which also includes the Cys biosynthesis enzyme O-acetylserine sulfhydrylase (OASS), but how the BSAS evolved distinct metabolic functions is not understood. Here we show that soybean (Glycine max) CAS and OASS form alpha-aminoacrylate reaction intermediates from Cys and O-acetylserine, respectively. To understand the molecular evolution of CAS and OASS in the BSAS enzyme family, the crystal structures of Gm-CAS and the Gm-CAS K95A mutant with a linked pyridoxal phosphate (PLP)-Cys molecule in the active site were determined. These structures establish a common fold for the plant BSAS family and reveal a substrate-induced conformational change that encloses the active site for catalysis. Comparison of CAS and OASS identified residues that covary in the PLP binding site. The Gm-OASS T81M, S181M, and T185S mutants altered the ratio of OASS:CAS activity but did not convert substrate preference to that of a CAS. Generation of a triple mutant Gm-OASS successfully switched reaction chemistry to that of a CAS. This study provides new molecular insight into the evolution of diverse enzyme functions across the BSAS family in plants.
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| Structure of Soybean beta-Cyanoalanine Synthase and the Molecular Basis for Cyanide Detoxification in Plants.,Yi H, Juergens M, Jez JM Plant Cell. 2012 Jun;24(6):2696-706. Epub 2012 Jun 26. PMID:22739827<ref>PMID:22739827</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 3vc3" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Cysteine synthase]]
| | [[Category: Glycine max]] |
| [[Category: Glycine hispida]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Jez, J M]] | | [[Category: Jez JM]] |
| [[Category: Yi, H]] | | [[Category: Yi H]] |
| [[Category: Beta-cyanoalanine synthase]]
| |
| [[Category: Transferase]]
| |