X-ray structures of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana.
X-ray structures of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana.
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Nfs2（来自拟南芥的质体半胱氨酸脱硫酶）的 X 射线结构。
DOI：
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
C. Didierjean
中科院分区：
文献类型：
--
作者：
T. Roret;H. Pégeot;Jérémy Couturier;G. Mulliert;N. Rouhier;C. Didierjean
拟南芥绿质体Nfs2 （AtNfs2）是II族吡多醛5'-磷酸依赖的半胱氨酸脱硫酶，参与铁硫簇生物发生的初始步骤。II族半胱氨酸脱硫酶需要硫转移酶如SufE蛋白的存在才能达到最佳活性。与I族半胱氨酸脱硫酶相比，该组蛋白含有含有催化半胱氨酸的更小的延伸叶，并具有限制活性位点的β-发夹。本文报道了AtNfs2的两种晶体结构：一种是野生型，催化半胱氨酸处于过硫-中间状态，另一种是C384S变体，模拟酶的静息状态。在这两种结构中，高度保守的Lys241共价结合吡哆醛5'-磷酸，形成内部醛胺。基于现有的同源细菌复合物，提出了AtNfs2与其生物伙伴AtSufE1的SufE结构域之间的复合物模型，揭示了结合位点的性质。
The chloroplastic Arabidopsis thaliana Nfs2 (AtNfs2) is a group II pyridoxal 5'-phosphate-dependent cysteine desulfurase that is involved in the initial steps of iron-sulfur cluster biogenesis. The group II cysteine desulfurases require the presence of sulfurtransferases such as SufE proteins for optimal activity. Compared with group I cysteine desulfurases, proteins of this group contains a smaller extended lobe harbouring the catalytic cysteine and have a β-hairpin constraining the active site. Here, two crystal structures of AtNfs2 are reported: a wild-type form with the catalytic cysteine in a persulfide-intermediate state and a C384S variant mimicking the resting state of the enzyme. In both structures the well conserved Lys241 covalently binds pyridoxal 5'-phosphate, forming an internal aldimine. Based on available homologous bacterial complexes, a model of a complex between AtNfs2 and the SufE domain of its biological partner AtSufE1 is proposed, revealing the nature of the binding sites.
一致。
DOI：
10.1097/iae.0000000000001602
发表时间：
2017
期刊：
Retina (Philadelphia, Pa.)
影响因子：
--
作者：
Todorich,Bozho;Thanos,Aristomenis;Yonekawa,Yoshihiro;Thomas,BenjaminJ;Faia,LisaJ;Chang,Emmanuel;Shulman,Julia;Olsen,KarlR;Blair,MichaelP;Shapiro,MichaelP;Ferrone,Philip;Vajzovic,Lejla;Toth,CynthiaA;Lee,ThomasC;Robinson,
通讯作者：
Robinson,
影响因子：
2.9
作者：
Kozakov, Dima;Beglov, Dmitri;Bohnuud, Tanggis;Mottarella, Scott E.;Xia, Bing;Hall, David R.;Vajda, Sandor
通讯作者：
Vajda, Sandor