Structural and biochemical analysis of a unique phosphatase from Bdellovibrio bacteriovorus reveals its structural and functional relationship with the protein tyrosine phosphatase class of phytase.
Structural and biochemical analysis of a unique phosphatase from Bdellovibrio bacteriovorus reveals its structural and functional relationship with the protein tyrosine phosphatase class of phytase.
复制标题
DOI：
10.1371/journal.pone.0094403
复制
发表时间：
2014
期刊：
影响因子：
3.7
通讯作者：
Lovering AL
中科院分区：
文献类型：
--
作者：
Gruninger RJ;Thibault J;Capeness MJ;Till R;Mosimann SC;Sockett RE;Selinger BL;Lovering AL
蜈蚣弧菌是一种罕见的δ变形杆菌，能入侵和捕食其他革兰氏阴性菌，作为一种治疗人、动物和农作物病原体的全细胞药物具有潜在的应用价值。蛋白酪氨酸磷酸酶(PTPs)是一类重要的酶，参与多种底物的脱磷作用，通常与细胞信号转导有关。细菌杆菌的开放阅读框Bd1204被预测编码一个未知功能的PTP。BD1204在结构和力学上都与类PTP植酸酶(PTPLP)相关，并具有许多迄今为止在任何其他PTPLP中未观察到的独特性质。BD1204对一些常见的蛋白质酪氨酸磷酸酶底物没有催化活性，但对六磷酸肌醇的磷酸单酯键具有高度的特异性。结构表明，Bd1204具有迄今为止所有表征的PTPLP中最小和最少的正电活性部位，但具有独特的底物专一性，其特征是对六磷酸肌醇具有严格的偏好。这两个活性部位的特征被认为是植酸降解酶专一性的最重要因素。我们推测Bd1204可能参与了猎物以外的磷酸盐获取。
Bdellovibrio bacteriovorus is an unusual δ-proteobacterium that invades and preys on other Gram-negative bacteria and is of potential interest as a whole cell therapeutic against pathogens of man, animals and crops. PTPs (protein tyrosine phosphatases) are an important class of enzyme involved in desphosphorylating a variety of substrates, often with implications in cell signaling. The B. bacteriovorus open reading frame Bd1204 is predicted to encode a PTP of unknown function. Bd1204 is both structurally and mechanistically related to the PTP-like phytase (PTPLP) class of enzymes and possesses a number of unique properties not observed in any other PTPLPs characterized to date. Bd1204 does not display catalytic activity against some common protein tyrosine phosphatase substrates but is highly specific for hydrolysis of phosphomonoester bonds of inositol hexakisphosphate. The structure reveals that Bd1204 has the smallest and least electropositive active site of all characterized PTPLPs to date yet possesses a unique substrate specificity characterized by a strict preference for inositol hexakisphosphate. These two active site features are believed to be the most significant contributors to the specificity of phytate degrading enzymes. We speculate that Bd1204 may be involved in phosphate acquisition outside of prey.
登录
查看更多内容
影响因子：
11
作者：
Pasternak, Zohar;Pietrokovski, Shmuel;Jurkevitch, Edouard
通讯作者：
Jurkevitch, Edouard
影响因子：
5.4
作者：
Gruninger, Robert J.;Selinger, L. Brent;Mosimann, Steven C.
通讯作者：
Mosimann, Steven C.
影响因子：
4.8
作者：
Gruninger, Robert J.;Dobing, Selina;Mosimann, Steven C.
通讯作者：
Mosimann, Steven C.
DOI：
10.1107/s0907444909052925
发表时间：
2010-02
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者：
Zwart PH
DOI：
10.1016/j.bbrc.2003.09.176
发表时间：
2003-12-05
影响因子：
3.1
作者：
Mullaney, EJ;Ullah, AHJ
通讯作者：
Ullah, AHJ