Backbone 1H, 13C, 15N NMR assignments of the unliganded and substrate ternary complex forms of mevalonate diphosphate decarboxylase from Streptococcus pneumoniae.
Backbone 1H, 13C, 15N NMR assignments of the unliganded and substrate ternary complex forms of mevalonate diphosphate decarboxylase from Streptococcus pneumoniae.
复制标题
肺炎链球菌甲羟戊酸二磷酸脱羧酶的未配体和底物三元复合物形式的主链 1H、13C、15N NMR 归属。
DOI：
10.1007/s12104-010-9255-4
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发表时间：
2011
影响因子：
0.9
通讯作者：
Leyh,ThomasS
中科院分区：
文献类型：
--
作者：
Reuther,Guido;Harris,Richard;Girvin,Mark;Leyh,ThomasS
甲氧丙酮二磷酸脱羧酶(MDD)催化二磷酸甘油酯(DPM)依赖于三磷酸腺苷(ATP)的脱羧基反应生成异戊烯基二磷酸(IPP)，它是25,000多种不同异戊二烯类化合物(包括胆固醇、类固醇激素和萜类化合物)的“构建块”。在这里，我们提出了肺炎链球菌MDD的第一个骨架归属，它处于未连接状态，并与DPM和AMPPCP--一种不能转移γ-磷酰基的核苷酸类似物--形成一个三元复合体。未连接形式的二级化学位移与化脓性链球菌的晶体结构一致(~70%的序列同源性)。底物和核苷酸的加入导致了与结合口袋中残基相对应的交叉峰的化学位移变化。
Mevalonate diphosphate decarboxylase (MDD) catalyzes the ATP-dependent decarboxylation of diphosphomevalonate (DPM) to produce isopentenyl diphosphate (IPP), the molecular “building block” for more than 25,000 distinct isoprenoids, including cholesterol, steroid hormones and terpenoids. Here, we present the first backbone assignment ofStreptococcus pneumoniaeMDD in the unliganded state and in a ternary complex with DPM and AMPPCP––a nucleotide analogue unable to transfer the γ-phosphoryl group. The secondary chemical shifts for the unliganded form are in good agreement with the crystal structure ofStreptococcus pyogenes(~70% sequence identity). The addition of substrate and nucleotide to the enzyme results in chemical shift changes of cross peaks that correspond to residues in the binding pocket.