3vbe: Difference between revisions
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New page: '''Unreleased structure''' The entry 3vbe is ON HOLD Authors: Yi, H., Jez, J.M. Description: Crystal structure of beta-cyanoalanine synthase in soybean |
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==Crystal structure of beta-cyanoalanine synthase in soybean== | |||
<StructureSection load='3vbe' size='340' side='right'caption='[[3vbe]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vbe]] is a 4 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=3VBE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VBE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | |||
<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=3vbe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vbe OCA], [https://pdbe.org/3vbe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vbe RCSB], [https://www.ebi.ac.uk/pdbsum/3vbe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vbe ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/I1L6I6_SOYBN I1L6I6_SOYBN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3vbe" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Glycine max]] | |||
[[Category: Large Structures]] | |||
[[Category: Jez JM]] | |||
[[Category: Yi H]] | |||
Latest revision as of 22:49, 26 March 2025
Crystal structure of beta-cyanoalanine synthase in soybean
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