Crystal structure of the cysteine desulfurase DndA from Streptomyces lividans which is involved in DNA phosphorothioation.

Crystal structure of the cysteine desulfurase DndA from Streptomyces lividans which is involved in DNA phosphorothioation.
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浅青紫链霉菌中参与 DNA 硫代磷酸化的半胱氨酸脱硫酶 DndA 的晶体结构

DOI:
10.1371/journal.pone.0036635
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发表时间:
2012
期刊:
影响因子:
3.7
通讯作者:
Wu G
Wu G
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Chen F;Zhang Z;Lin K;Qian T;Zhang Y;You D;He X;Wang Z;Liang J;Deng Z;Wu G

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DNA phosphorothioation is widespread among prokaryotes, and might function to restrict gene transfer among different kinds of bacteria. There has been little investigation into the structural mechanism of the DNA phosphorothioation process. DndA is a cysteine desulfurase which is involved in the first step of DNA phosphorothioation. In this study, we determined the crystal structure of Streptomyces lividans DndA in complex with its covalently bound cofactor PLP, to a resolution of 2.4 Å. Our structure reveals the molecular mechanism that DndA employs to recognize its cofactor PLP, and suggests the potential binding site for the substrate L-cysteine on DndA. In contrast to previously determined structures of cysteine desulfurases, the catalytic cysteine of DndA was found to reside on a β strand. This catalytic cysteine is very far away from the presumable location of the substrate, suggesting that a conformational change of DndA is required during the catalysis process to bring the catalytic cysteine close to the substrate cysteine. Moreover, our in vitro enzymatic assay results suggested that this conformational change is unlikely to be a simple result of random thermal motion, since moving the catalytic cysteine two residues forward or backward in the primary sequence completely disabled the cysteine desulfurase activity of DndA.
DOI: 10.1107/s0907444904019158
发表时间: 2004-12-01
影响因子: 2.2
作者:
Emsley, P;Cowtan, K
通讯作者: Cowtan, K
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发表时间: 1993-04-01
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DOI: 10.1371/journal.pone.0005132
发表时间: 2009
期刊: PloS one
影响因子: 3.7
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