Structural insights into auxiliary cofactor usage by radical S-adenosylmethionine enzymes.
Structural insights into auxiliary cofactor usage by radical S-adenosylmethionine enzymes.
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DOI：
10.1016/j.cbpa.2022.102153
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发表时间：
2022-06
影响因子：
7.8
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中科院分区：
文献类型：
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Radical S-adenosylmethionine (SAM) enzymes use a common catalytic core for diverse transformations. While all radical SAM enzymes bind a Fe4S4 cluster via a characteristic tri-cysteine motif, many bind additional metal cofactors. Recently reported structures of radical SAM enzymes that use methylcobalamin or additional iron-sulfur clusters as cosubstrates show that these auxiliary units are anchored by N- and C-terminal domains that vary significantly in size and topology. Despite this architectural diversity, all use a common surface for auxiliary cofactor docking. In the sulfur insertion and metallocofactor assembly systems evaluated here, interaction with iron-sulfur cluster assembly proteins or downstream scaffold proteins is an important component of catalysis. Structures of these complexes represent important new frontiers in structural analysis of radical SAM enzymes.
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影响因子：
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DOI：
10.1073/pnas.1703663114
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