Crystal structure of the cystine C-S lyase from Synechocystis:: Stabilization of cysteine persulfide for FeS cluster biosynthesis
Crystal structure of the cystine C-S lyase from Synechocystis:: Stabilization of cysteine persulfide for FeS cluster biosynthesis
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DOI：
10.1073/pnas.97.8.3856
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发表时间：
2000-04-11
影响因子：
11.1
通讯作者：
Kessler, D
中科院分区：
文献类型：
--
作者：
Clausen, T;Kaiser, JT;Kessler, D
FeS簇是多种蛋白质的多功能辅因子，但其生物合成机制仍然未知。来自集胞藻的胱氨酸C-S裂解酶已被鉴定为铁氧还蛋白FeS簇形成的参与者。在这里，我们报告的晶体结构的裂解酶和复杂的反应产物的胱氨酸裂解在1.8-和1.55-埃分辨率，分别。含硫产物被明确鉴定为过硫化半胱氨酸。反应性过硫化物基团通过氢键固定到疏水口袋中心的His-114上，从而与溶剂隔离。半胱氨酸过硫化物的结合和稳定化代表了通过NifS样蛋白产生蛋白质结合的过硫化物的替代方案，并指出过硫化物化合物对于FeS簇组装的普遍重要性。
FeS clusters are versatile cofactors of a variety of proteins, but the mechanisms of their biosynthesis are still unknown. The cystine C-S lyase from Synechocystis has been identified as a participant in ferredoxin FeS cluster formation. Herein, we report on the crystal structure of the lyase and of a complex with the reaction products of cystine cleavage at 1.8- and 1.55-Angstrom resolution, respectively. The sulfur-containing product was unequivocally identified as cysteine persulfide. The reactive persulfide group is fixed by a hydrogen bond to His-114 in the center of a hydrophobic pocket and is thereby shielded from the solvent. Binding and stabilization of the cysteine persulfide represent an alternative to the generation of a protein-bound persulfide by NifS-like proteins and point to the general importance of persulfidic compounds for FeS cluster assembly.