pH-tuneable binding of 2 '-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study

Ciulli A; Lobley CMC; Tuck KLSmith AGBlundell TLAbell C

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pH-tuneable binding of 2 '-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study

机译：2的-phospho-ADP-ribose pH-tuneable绑定ketopantoate还原酶:结构和量热研究

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The crystal structure of Escherichia coli ketopantoate reductase in complex with 2'-monophosphoadenosine 5'-diphosphoribose, a fragment of NADP+ that lacks the nicotinamide ring, is reported. The ligand is bound at the enzyme active site in the opposite orientation to that observed for NADP+, with the adenine ring occupying the lipophilic nicotinamide pocket. Isothermal titration calorimetry with R31A and N98A mutants of the enzyme is used to show that the unusual 'reversed binding mode' observed in the crystal is triggered by changes in the protonation of binding groups at low pH. This research has important implications for fragment-based approaches to drug design, namely that the crystallization conditions and the chemical modification of ligands can have unexpected effects on the binding modes.

机译：大肠杆菌的晶体结构ketopantoate还原酶在复杂2 -monophosphoadenosine 5 -diphosphoribose, a片段的NADP +缺乏烟酰胺戒指,据报道。酶活性部位在相反的方向观察辅酶ii +,腺嘌呤环占领了亲脂性的烟酰胺的口袋里。等温滴定与R31A和量热法N98A酶的突变体是用来显示不寻常的逆转绑定模式中观察到晶体是由变化引起的绑定组的质子化作用在低博士研究有重要意义fragment-based药物设计方法,即和结晶的条件配体的化学改性意想不到的对绑定模式的影响。

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来源
《Acta crystallographica.Section D. Biological crystallography》 |2007年第2期|171-178|共8页
作者
Ciulli A; Lobley CMC; Tuck KLSmith AGBlundell TLAbell C;
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作者单位

Univ Cambridge, Dept Plant Sci, Cambridge CB2 3EA, England;

Univ Cambridge, Chem Lab, Cambridge CB2 1EW, England;

Univ Cambridge, Dept Biochem, Cambridge CB2 1GA, England;

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正文语种英语
中图分类化学;
关键词
biosynthesis; crystal structure; isothermal titration calorimetryCrystallography2-dehydropantoate 2-reductaseDrug DiscoveryNiacinamideenzyme active site;

机译：生物合成;晶体结构;等温过程滴定法calorimetryCrystallography2-dehydropantoate2-reductaseDrug DiscoveryNiacinamideenzyme活跃网站;

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pH-tuneable binding of 2 '-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study

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