Structural and biochemical analyses of Microcystis aeruginosa O-acetylserine sulfhydrylases reveal a negative feedback regulation of cysteine biosynthesis
العنوان: | Structural and biochemical analyses of Microcystis aeruginosa O-acetylserine sulfhydrylases reveal a negative feedback regulation of cysteine biosynthesis |
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المؤلفون: | Bo-Ying Xu, Yuxing Chen, Wang Cheng, Kang Zhou, Mo Lu, Yong-Liang Jiang, Cong-Zhao Zhou |
المصدر: | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844:308-315 |
بيانات النشر: | Elsevier BV, 2014. |
سنة النشر: | 2014 |
مصطلحات موضوعية: | Models, Molecular, Microcystis, Protein Conformation, Stereochemistry, Molecular Sequence Data, Biophysics, Cystine, Biology, Crystallography, X-Ray, Biochemistry, Analytical Chemistry, chemistry.chemical_compound, Catalytic Domain, Microcystis aeruginosa, Amino Acid Sequence, Cysteine, Cloning, Molecular, Binding site, Molecular Biology, Gene, Feedback, Physiological, chemistry.chemical_classification, Cysteine Synthase, Sequence Homology, Amino Acid, Substrate (chemistry), Molecular Sequence Annotation, biology.organism_classification, Enzyme, chemistry, O-Acetylserine, Bacteria |
الوصف: | article i nfo O-acetylserine sulfhydrylase (OASS) catalyzes the final step of cysteine biosynthesis from O-acetylserine (OAS) and inorganic sulfide in plants and bacteria. Bioinformatics analyses combined with activity assays enabled us to annotate the two putative genes of Microcystis aeruginosa PCC 7806 to CysK1 and CysK2, which encode the two 75% sequence-identical OASS paralogs. Moreover, we solved the crystal structures of CysK1 at 2.30 Ǻ and cystine-complexed CysK2 at 1.91 Ǻ, revealing a quite similar overall structure that belongs to the family of fold-type II PLP-dependent enzymes. Structural comparison indicated a significant induced fi tu pon binding to the cystine, which occupies the binding site for the substrate OAS and blocks the product release tunnel. Subsequent enzymatic assays further confirmed that cystine is a competitive inhibitor of the substrate OAS. Moreover, multiple-sequence alignment revealed that the cystine-binding residues are highly conserved in all OASS proteins, suggesting that this auto-inhibition of cystine might be a universal mechanism of cysteine biosynthesis pathway. |
تدمد: | 1570-9639 |
URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3592ecd070112c49657e8b551d1575d https://doi.org/10.1016/j.bbapap.2013.11.008 |
حقوق: | CLOSED |
رقم الأكسشن: | edsair.doi.dedup.....b3592ecd070112c49657e8b551d1575d |
قاعدة البيانات: | OpenAIRE |
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