High-resolution crystal structure of copper amine oxidase from Arthrobacter globiformis: Assignment of bound diatomic molecules as O2

MurakawaT.; HayashiH.; SunamiT.KuriharaK.TamadaT.KurokiR.SuzukiM.TanizawaK.OkajimaT.

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High-resolution crystal structure of copper amine oxidase from Arthrobacter globiformis: Assignment of bound diatomic molecules as O2

机译：高分辨率的晶体结构的铜胺氧化酶从节细菌属globiformis:任务绑定双原子分子的O2

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The crystal structure of a copper amine oxidase from Arthrobacter globiformis was determined at 1.08 ? resolution with the use of low-molecular-weight polyethylene glycol (LMW PEG; average molecular weight ～200) as a cryoprotectant. The final crystallographic R factor and R free were 13.0 and 15.0%, respectively. Several molecules of LMW PEG were found to occupy cavities in the protein interior, including the active site, which resulted in a marked reduction in the overall B factor and consequently led to a subatomic resolution structure for a relatively large protein with a monomer molecular weight of ～70 000. About 40% of the presumed H atoms were observed as clear electron densities in the Fo - Fc difference map. Multiple minor conformers were also identified for many residues. Anisotropic displacement fluctuations were evaluated in the active site, which contains a post-translationally derived quinone cofactor and a Cu atom. Furthermore, diatomic molecules, most likely to be molecular oxygen, are bound to the protein, one of which is located in a region that had previously been proposed as an entry route for the dioxygen substrate from the central cavity of the dimer interface to the active site.

机译：铜的晶体结构胺氧化酶从节细菌属globiformis决心1.08 ?低分子量聚乙二醇(流明瓦挂钩;冷冻保护剂。因素和R免费13.0和15.0%,分别。在蛋白质内部,发现占领蛀牙包括活性部位,导致标志着整个B因子和减少因此导致了亚原子决议为一个相对较大的蛋白质结构单体分子量000 ~ 70。假定H原子观察清楚电子密度的Fo - Fc不同地图。多个小矫形器也被确定对于许多残留。波动在活性部位进行评估,它包含一个你导出吗醌代数余子式和一个铜原子。双原子分子,最有可能的分子氧气,绑定到蛋白质,其中一个是位于一个以前的地区提出了分子氧的路由条目二聚体的底物从中央腔界面活性部位。

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《Acta crystallographica.Section D. Biological crystallography》 |2013年第12期|2483-2494|共12页
作者
MurakawaT.; HayashiH.; SunamiT.KuriharaK.TamadaT.KurokiR.SuzukiM.TanizawaK.OkajimaT.;
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作者单位

Department of Chemistry, Osaka Medical College, 2-7 Daigakumachi, Takatsuki, Osaka 569-8686, Japan;

Institute of Scientific and Industrial Research, Osaka University, 8-1 Mihogaoka, Ibaraki, Osaka;

Molecular Structural Biology Group, Quantum Beam Science Directorate, Japan Atomic Energy Agency, 2Department of Biochemistry, Osaka Medical College, 2-7 Daigakumachi, Takatsuki, Osaka 569-8686Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan;

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正文语种英语
中图分类化学;
关键词
oxygen; Amine Oxidase (Copper-Containing); Molecular weightscrystal structureDiatomic moleculesDioxygenArthrobacter globiformisActive Site;

机译：氧气;胺氧化酶(铜);分子weightscrystal structureDiatomicmoleculesDioxygenArthrobacter globiformisActive网站;

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High-resolution crystal structure of copper amine oxidase from Arthrobacter globiformis: Assignment of bound diatomic molecules as O2

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