CryB from Rhodobacter sphaeroides: a unique class of cryptochromes with new cofactors
CryB from Rhodobacter sphaeroides: a unique class of cryptochromes with new cofactors
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DOI：
10.1038/embor.2012.2
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发表时间：
2012-03-01
期刊：
影响因子：
7.7
通讯作者：
Essen, Lars-Oliver
中科院分区：
文献类型：
--
作者：
Geisselbrecht, Yann;Fruehwirth, Sebastian;Essen, Lars-Oliver
隐花色素和光解酶在结构上相关，但在信号传导和DNA修复中具有不同的生物学功能。变形菌和蓝藻含有一类新的隐花色素，称为CryPro。我们已经解决了它的成员之一，隐花色素B从Rhodobacter sphaeroides，这是光合作用基因表达的调节器的2.7埃结构。结构表明，除了光裂合酶样折叠，CryB包含两个辅因子，仅在CryPro亚家族中保守：在触角结合结构域中的6，7-二甲基-8-核糖基-鲁马嗪和催化结构域内的[4Fe-4S]簇。后者非常相似的铁硫簇窝藏大引物酶亚基PriL，表明PriL是进化相关的CryPro类隐花色素。
Cryptochromes and photolyases are structurally related but have different biological functions in signalling and DNA repair. Proteobacteria and cyanobacteria harbour a new class of cryptochromes, called CryPro. We have solved the 2.7 angstrom structure of one of its members, cryptochrome B from Rhodobacter sphaeroides, which is a regulator of photosynthesis gene expression. The structure reveals that, in addition to the photolyase-like fold, CryB contains two cofactors only conserved in the CryPro subfamily: 6,7-dimethyl-8-ribityl-lumazine in the antenna-binding domain and a [4Fe-4S] cluster within the catalytic domain. The latter closely resembles the iron-sulphur cluster harbouring the large primase subunit PriL, indicating that PriL is evolutionarily related to the CryPro class of cryptochromes.