Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii.
Crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii.
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来自嗜热栖热菌、托科代硫化叶菌和詹氏甲烷球菌的甲酰甘酰胺核糖核苷酸酰胺转移酶 PurS 亚基的晶体结构。
DOI：
10.1107/s2053230x1600978x
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发表时间：
2016
期刊：
影响因子：
--
通讯作者：
and Kawai G.
中科院分区：
文献类型：
--
作者：
Watanabe Y.;Yanai H.;Kanagawa M.;Suzuki S.;Tamura S.;Okada K.;Baba S.;Kumasaka T.;Agari Y.;Chen L.;Fu Z. Q.;Chrzas J.;Wang B. C.;Nakagawa N.;Ebihara A.;Masui R.;Kuramitsu S.;Yokoyama S.;Sampei G. I.;and Kawai G.
测定了嗜热栖热菌（Thermus thermophilus）、东京硫化叶菌（Sulfolobus tokodaii）和詹氏甲烷球菌（Methanocaldococcus jannaschii）的甲酰甘氨酰胺核苷酸转酰胺酶（PurS）亚基的晶体结构，并分析了其结构特征。对于来自T的PurS。在嗜热菌中，使用在不同条件下生长的两种晶体确定两种结构。二聚体形式的四种结构几乎彼此相同，尽管它们的序列同一性相对较低。这也适用于迄今为止确定的所有PurS结构。几个残基是保守的PurSs之间，这些都位于与PurL和PurQ，甲酰甘氨酰胺核糖核苷酸酰胺转移酶的其他亚基的相互作用位点。PurS二聚体的分子动力学模拟以及PurS二聚体，PurL和PurQ的复合物的模型表明，PurS通过其弯曲运动在酶的催化中起着一定的作用。
The crystal structures of a subunit of the formylglycinamide ribonucleotide amidotransferase, PurS, from Thermus thermophilus, Sulfolobus tokodaii and Methanocaldococcus jannaschii were determined and their structural characteristics were analyzed. For PurS from T. thermophilus, two structures were determined using two crystals that were grown in different conditions. The four structures in the dimeric form were almost identical to one another despite their relatively low sequence identities. This is also true for all PurS structures determined to date. A few residues were conserved among PurSs and these are located at the interaction site with PurL and PurQ, the other subunits of the formylglycinamide ribonucleotide amidotransferase. Molecular-dynamics simulations of the PurS dimer as well as a model of the complex of the PurS dimer, PurL and PurQ suggest that PurS plays some role in the catalysis of the enzyme by its bending motion.