Structure of the branched-chain aminotransferase from Streptococcus mutans

RuanJ.; HuJ.; YinA.WuW.CongX.FengX.LiS.

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Structure of the branched-chain aminotransferase from Streptococcus mutans

机译：支链氨基转移酶的结构从变形链球菌

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The branched-chain amino-acid aminotransferase from Streptococcus mutans (SmIlvE) was recombinantly expressed in Escherichia coli with high yield. An effective purification protocol was established. A bioactivity assay indicated that SmIlvE had aminotransferase activity. The specific activity of SmIlvE towards amino-acid substrates was found to be as follows (in descending order): Ile >Leu >Val >Trp >Gly. The protein was crystallized using the hanging-drop vapour-diffusion method with PEG 3350 as the primary precipitant. The structure of SmIlvE was solved at 1.97 ?resolution by the molecular-replacement method. Comparison with structures of homologous proteins enabled the identification of conserved structural elements that might play a role in substrate binding. Further work is needed to confirm the interaction between SmIlvE and its substrates by determining the structures of their complexes.

机译：的支链氨基酸转氨酶从变形链球菌(SmIlvE)重组大肠杆菌中表达高收益。成立。SmIlvE转氨酶活性。对氨基酸SmIlvE的特定活动底物被发现如下(在降序排列):Ile >低浓缩铀> Val > Trp > g。使用悬滴蛋白质结晶vapour-diffusion方法与3350年挂钩主要的沉淀剂。解决在1.97 ?决议的molecular-replacement方法。使结构的同源蛋白质守恒的结构元素的识别这可能在衬底中扮演一个角色绑定。需要进一步研究来证实的交互SmIlvE及其基板之间通过确定他们的配合物的结构。

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来源
《Acta crystallographica.Section D. Biological crystallography》 |2012年第8期|996-1002|共7页
作者
RuanJ.; HuJ.; YinA.WuW.CongX.FengX.LiS.;
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作者单位

Department of Immunology, School of Basic Medical Sciences, Capital Medical University, Beijing;

Medical Experiment and Test Centre, Capital Medical University, Beijing 100069, China;

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正文语种英语
中图分类化学;
关键词
Structural elements; Streptococcus mutans; Transaminases;

机译：结构元素;链球菌变形链球菌;氨基转移酶;

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Structure of the branched-chain aminotransferase from Streptococcus mutans

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