9vsm: Difference between revisions

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'''Unreleased structure'''


The entry 9vsm is ON HOLD  until Paper Publication
==Crystal structure of cystathionine gamma-synthase from Lactobacillus plantarum complexed with the cystathionine-bound external aldimine==
<StructureSection load='9vsm' size='340' side='right'caption='[[9vsm]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vsm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactiplantibacillus_plantarum_WCFS1 Lactiplantibacillus plantarum WCFS1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VSM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VSM 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]] 1.58&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=E9U:(2~{S})-4-[(2~{R})-2-azanyl-3-oxidanyl-3-oxidanylidene-propyl]sulfanyl-2-[(~{E})-[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]butanoic+acid'>E9U</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=9vsm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vsm OCA], [https://pdbe.org/9vsm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vsm RCSB], [https://www.ebi.ac.uk/pdbsum/9vsm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vsm ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cystathionine gamma-synthase (CGS) and cystathionine gamma-lyase (CGL) have highly similar amino acid sequences. CGS catalyzes the generation of cystathionine from acylated l-homoserine and l-cysteine, whereas CGL catalyzes the decomposition of cystathionine to produce l-cysteine. Lactobacillus plantarum is a unique bacterium containing two open reading frames of CGL/CGS enzymes in its genome. Structural studies of LpCGS and LpCGL may provide insights into their reaction specificities. In the present study, we elucidated the structure and enzymatic function of LpCGS. We found that LpCGS has substrate specificity toward acetylated rather than succinylated l-homoserine. LpCGS has the characteristic residues E55 and V232 in the substrate-binding pocket, which synergistically confer substrate specificity toward acetylated l-homoserine. These results may facilitate the development of inhibitors of l-methionine and l-cysteine biosynthetic pathways.


Authors:  
Structural insight into the substrate specificity of cystathionine gamma-synthase from Lactobacillus plantarum.,Matoba Y, Oda K, Ohtani M, Mende Y, Noda K FEBS Lett. 2026 Jan 21. doi: 10.1002/1873-3468.70276. PMID:41562399<ref>PMID:41562399</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9vsm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lactiplantibacillus plantarum WCFS1]]
[[Category: Large Structures]]
[[Category: Matoba Y]]
[[Category: Oda K]]
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