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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structures of apo and GTP-bound molybdenum cofactor biosynthesis protein MoaC from Thermus thermophilus HB8.
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Structures of apo and GTP-bound molybdenum cofactor biosynthesis protein MoaC from Thermus thermophilus HB8.

机译：结构的和GTP-bound钼代数余子式生物合成蛋白质MoaC栖热菌属酸奶有助于HB8。

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摘要

The first step in the molybdenum cofactor (Moco) biosynthesis pathway involves the conversion of guanosine triphosphate (GTP) to precursor Z by two proteins (MoaA and MoaC). MoaA belongs to the S-adenosylmethionine-dependent radical enzyme superfamily and is believed to generate protein and/or substrate radicals by reductive cleavage of S-adenosylmethionine using an Fe-S cluster. MoaC has been suggested to catalyze the release of pyrophosphate and the formation of the cyclic phosphate of precursor Z. However, structural evidence showing the binding of a substrate-like molecule to MoaC is not available. Here, apo and GTP-bound crystal structures of MoaC from Thermus thermophilus HB8 are reported. Furthermore, isothermal titration calorimetry experiments have been carried out in order to obtain thermodynamic parameters for the protein-ligand interactions. In addition, molecular-dynamics (MD) simulations have been carried out on the protein-ligand complex of known structure and on models of relevant complexes for which X-ray structures are not available. The biophysical, structural and MD results reveal the residues that are involved in substrate binding and help in speculating upon a possible mechanism.
机译：的第一步钼辅因子(岩豚鼠)生物合成途径涉及到的转换三磷酸鸟苷(三磷酸鸟苷)前体Z两种蛋白质(MoaA和MoaC)。S-adenosylmethionine-dependent激进的酶总科和被认为产生蛋白质和/或底物还原裂解自由基的S-adenosylmethionine使用Fe-S集群。MoaC建议促进释放焦磷酸和循环的形成然而,磷酸盐的前体z结构证据显示substrate-like绑定分子MoaC是不可用的。GTP-bound MoaC从栖热菌属的晶体结构酸奶有助于HB8报告。等温滴定量热学实验进行为了获得热力学参数protein-ligand交互。此外,分子动力学(MD)模拟进行了在protein-ligand吗复杂的结构和模型有关x射线结构的复合体不可用。结果揭示了参与的残留物衬底绑定和帮助在投机可能的机制。

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