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首页> 外文期刊>Journal of Molecular Biology >Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes.
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Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes.

机译：模块化FAD合成酶晶体结构中的低聚状态提供了对其在原核生物中顺序催化的了解。

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摘要

The crystal structure of the modular flavin adenine dinucleotide (FAD) synthetase from Corynebacterium ammoniagenes has been solved at 1.95 A resolution. The structure of C. ammoniagenes FAD synthetase presents two catalytic modules-a C-terminus with ATP-riboflavin kinase activity and an N-terminus with ATP-flavin mononucleotide (FMN) adenylyltransferase activity-that are responsible for the synthesis of FAD from riboflavin in two sequential steps. In the monomeric structure, the active sites from both modules are placed 40 A away, preventing the direct transfer of the product from the first reaction (FMN) to the second catalytic site, where it acts as substrate. Crystallographic and biophysical studies revealed a hexameric assembly formed by the interaction of two trimers. Each trimer presents a head-tail configuration, with FMN adenylyltransferase and riboflavin kinase modules from different protomers approaching the active sites and allowing the direct transfer of FMN. Experimental results provide molecular-level evidences of the mechanism of the synthesis of FMN and FAD in prokaryotes in which the oligomeric state could be involved in the regulation of the catalytic efficiency of the modular enzyme.
机译：来自产氨棒杆菌的模块化黄素腺嘌呤二核苷酸（FAD）合成酶的晶体结构已在1.95 A的分辨率下解析。氨化衣原体FAD合成酶的结构呈现两个催化模块-一个具有ATP-核黄素激酶活性的C末端和一个具有ATP-黄素单核苷酸（FMN）腺苷酸转移酶活性的N末端-负责由核黄素合成FAD两个连续步骤。在单体结构中，两个模块的活性位点相距40 A，以防止产物直接从第一反应（FMN）转移到第二催化位点，在该处充当底物。晶体学和生物物理研究揭示了由两个三聚体相互作用形成的六聚体组装体。每个三聚体均呈头尾构型，来自不同原初的FMN腺苷酸转移酶和核黄素激酶模块接近活性位点，并允许FMN的直接转移。实验结果为原核生物中FMN和FAD的合成机理提供了分子水平的证据，其中寡聚态可能参与了模块化酶催化效率的调节。

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