The NMR contribution to protein-protein networking in Fe-S protein maturation.
The NMR contribution to protein-protein networking in Fe-S protein maturation.
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DOI：
10.1007/s00775-018-1552-x
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发表时间：
2018-06
期刊：
影响因子：
--
通讯作者：
Piccioli M
中科院分区：
文献类型：
--
作者：
Banci L;Camponeschi F;Ciofi-Baffoni S;Piccioli M
铁硫蛋白是利用顺磁系统定制的核磁共振波谱进行积极研究的第一类金属蛋白之一。超精细位移、它们的温度依赖性和簇结合残基的核弛豫速率是 Fe-S 簇的性质和氧化态的有效指纹。 NMR 极大地促进了磁耦合模式的分析以及对与蛋白质结合的 [2Fe-2S]、[3Fe-4S] 和 [4Fe-4S] 簇中发生的电子结构的理解。在获得还原 E. halophila HiPIP I 的顺磁蛋白的第一个 NMR 结构后，确定了几种不同氧化态的 Fe-S 蛋白的许多 NMR 结构。研究发现，化学位移、未观察到的残基模式、内部迁移率和热力学稳定性方面的差异是绘制蛋白质两种不同氧化态之间细微变化的合适数据。最近，通过将溶液核磁共振标准实验与顺磁系统定制的实验相结合，对负责成熟人类线粒体和胞质 Fe-S 蛋白的相互作用网络进行了很大程度上的表征。我们在这里展示了溶液核磁共振在提供“Fe-S相互作用组学”的详细分子视图方面的贡献。当蛋白质-蛋白质相互作用较弱且短暂，因此难以用其他方法以高分辨率进行表征时，这种贡献特别有效。
Iron–sulfur proteins were among the first class of metalloproteins that were actively studied using NMR spectroscopy tailored to paramagnetic systems. The hyperfine shifts, their temperature dependencies and the relaxation rates of nuclei of cluster-bound residues are an efficient fingerprint of the nature and the oxidation state of the Fe–S cluster. NMR significantly contributed to the analysis of the magnetic coupling patterns and to the understanding of the electronic structure occurring in [2Fe–2S], [3Fe–4S] and [4Fe–4S] clusters bound to proteins. After the first NMR structure of a paramagnetic protein was obtained for the reduced E. halophila HiPIP I, many NMR structures were determined for several Fe–S proteins in different oxidation states. It was found that differences in chemical shifts, in patterns of unobserved residues, in internal mobility and in thermodynamic stability are suitable data to map subtle changes between the two different oxidation states of the protein. Recently, the interaction networks responsible for maturing human mitochondrial and cytosolic Fe–S proteins have been largely characterized by combining solution NMR standard experiments with those tailored to paramagnetic systems. We show here the contribution of solution NMR in providing a detailed molecular view of “Fe–S interactomics”. This contribution was particularly effective when protein–protein interactions are weak and transient, and thus difficult to be characterized at high resolution with other methodologies.
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影响因子：
16.6
作者：
Beilschmidt LK;Ollagnier de Choudens S;Fournier M;Sanakis I;Hograindleur MA;Clémancey M;Blondin G;Schmucker S;Eisenmann A;Weiss A;Koebel P;Messaddeq N;Puccio H;Martelli A
通讯作者：
Martelli A
影响因子：
2.9
作者：
Bertini, I;Cowan, JA;Piccioli, M
通讯作者：
Piccioli, M
DOI：
10.1016/0005-2728(75)90132-2
发表时间：
1975-01-01
期刊：
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子：
--
作者：
ANDERSON, RE;DUNHAM, WR;CRESPI, HL
通讯作者：
CRESPI, HL
影响因子：
2.9
作者：
Aono, S;Bentrop, D;Rosato, A
通讯作者：
Rosato, A
DOI：
10.1111/j.1432-1033.1996.00092.x
发表时间：
1996-02-15
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
Bentrop, D;Bertini, I;Teixeira, M
通讯作者：
Teixeira, M