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首页> 外文期刊>Journal of Molecular Biology >Crystal structure of an ADP-dependent glucokinase from Pyrococcus furiosus: implications for a sugar-induced conformational change in ADP-dependent kinase.
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Crystal structure of an ADP-dependent glucokinase from Pyrococcus furiosus: implications for a sugar-induced conformational change in ADP-dependent kinase.

机译：激烈热球菌ADP依赖性葡萄糖激酶的晶体结构：对糖诱导的ADP依赖性激酶构象变化的影响。

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摘要

ADP-dependent kinases are used in the modified Embden-Meyerhoff pathway of certain archaea. Our previous study has revealed a mechanism for ADP-dependent phosphoryl transfer by Thermococcus litoralis glucokinase (tlGK), and its evolutionary relationship with ATP-dependent ribokinases and adenosine kinases (PFKB carbohydrate kinase family members). Here, we report the crystal structure of glucokinase from Pyrococcus furiosus (pfGK) in a closed conformation complexed with glucose and AMP at 1.9A resolution. In comparison with the tlGK structure, the pfGK structure shows significant conformational changes in the small domain and a region around the hinge, suggesting glucose-induced domain closing. A part of the large domain next to the hinge is also shifted accompanied with domain closing. In the pfGK structure, glucose binds in a groove between the large and small domains, and the electron density of O1 atoms for both the alpha and beta-anomer configurations was observed. The structural details of the sugar-binding site of ADP-dependent glucokinase were firstly clarified and then site-directed mutagenesis analysis clarified the catalytic residues for ADP-dependent kinase, such as Arg205 and Asp451 of tlGK. Homology search and multiple alignment of amino acid sequences using the information obtained from the structures reveals that eucaryotic hypothetical proteins homologous to ADP-dependent kinases retain the residues for the recognition of a glucose substrate.
机译：ADP依赖性激酶被用于某些古细菌的修饰的Embden-Meyerhoff途径。我们以前的研究已经揭示了利特尔热球菌葡萄糖激酶（tlGK）依赖ADP的磷酰基转移的机制，以及它与ATP依赖的核糖激酶和腺苷激酶（PFKB碳水化合物激酶家族成员）的进化关系。在这里，我们报告了激烈热球菌（pfGK）的葡萄糖激酶的晶体结构，其封闭构象与葡萄糖和AMP在1.9A分辨率下复合。与tlGK结构相比，pfGK结构在小结构域和铰链周围区域显示出显着的构象变化，表明葡萄糖诱导的结构域闭合。靠近铰链的大区域的一部分也会随着区域闭合而移动。在pfGK结构中，葡萄糖结合在大畴和小畴之间的凹槽中，并且观察到α和β端基异构体构型的O1原子的电子密度。首先阐明了ADP依赖性葡萄糖激酶的糖结合位点的结构细节，然后进行了定点诱变分析，阐明了ADP依赖性激酶的催化残基，例如tlGK的Arg205和Asp451。使用从结构获得的信息进行同源性搜索和氨基酸序列的多重比对揭示，与ADP依赖性激酶同源的真核假想蛋白质保留了用于识别葡萄糖底物的残基。

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