Cystathionine gamma synthase
FunctionCystathionine gamma synthase (CGS) catalyzes the formation of cystathionine and succinate from cysteine and succinyl homoserine in microorganisms and plants. This reaction is part of Met biosynthesis pathway[1]. RelevanceCGS deletion mutants in bacteria caused lack of growth which was reversed by addition of Met[2]. CGS is a target of antimicrobial agent and herbicides. Structural highlightsThe 3D structure of tobacco CGS complex with an inhibitor shows . The carboxylate moiety of the inhibitor makes hydrogen bond to and its [3].
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3D structures of cystathionine gamma synthase3D structures of cystathionine gamma synthase
Updated on 20-February-2025
1i41 - tCGS + inhibitor - tobacco
1qgn - tCGS + PLP
1i43, 1i48 - tCGS + PLP + inhibitor
1cs1 - CGS + PLP derivative - Eschericia coli
4l0o - CGS + PLP - Helicobacter pylori
6s0c - CGS + PLP - Citrobacter freundii
9axj - CGS + Pyridine derivative – Thermobifida fusca
3qi6, 3qhx - CGS MetB - Mycobacterium ulcerans
5x5h - CGS MetB - Corynebacterium glutamicum
6ld7 - XoCGS (mutant`) + PLP derivative - Xanthomonas oryzae
6ld9 - XoCGS (mutant`) + cystathionine
6ld8 - XoCGS (mutant`) + cysteine + aminoacrylate
6lgo - XoCGS (mutant`) + homolanthionine
ReferencesReferences
- ↑ Flavin M, Slaughter C. Enzymatic synthesis of homocysteine or methionine directly from O-succinyl-homoserine. Biochim Biophys Acta. 1967 Mar 15;132(2):400-5. doi:, 10.1016/0005-2744(67)90158-1. PMID:5340123 doi:http://dx.doi.org/10.1016/0005-2744(67)90158-1
- ↑ Fu J, Wu J, Jiang J, Wang Z, Ma Z. Cystathionine gamma-synthase is essential for methionine biosynthesis in Fusarium graminearum. Fungal Biol. 2013 Jan;117(1):13-21. doi: 10.1016/j.funbio.2012.11.001. Epub 2012 , Dec 1. PMID:23332829 doi:http://dx.doi.org/10.1016/j.funbio.2012.11.001
- ↑ Steegborn C, Laber B, Messerschmidt A, Huber R, Clausen T. Crystal structures of cystathionine gamma-synthase inhibitor complexes rationalize the increased affinity of a novel inhibitor. J Mol Biol. 2001 Aug 24;311(4):789-801. PMID:11518531 doi:10.1006/jmbi.2001.4880