Homology modeling of Mycoplasma pneumoniae enolase and its molecular interaction with human plasminogen.
Homology modeling of Mycoplasma pneumoniae enolase and its molecular interaction with human plasminogen.
复制标题
支原体肺炎烯醇酶的同源性建模及其与人纤溶酶原的分子相互作用。
DOI：
10.6026/97320630003018
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发表时间：
2008
期刊：
影响因子：
1.9
通讯作者：
Meksuriyen D
中科院分区：
文献类型：
--
作者：
Chumchua V;Pornputtapong N;Thammarongtham C;Meksuriyen D
α-烯醇化酶（α-enolase，e）是一种糖酵解酶，作为多种细菌的表面受体介导纤溶酶原（plasminogen，pg）结合。它也被认为是一些致病菌的毒力因子，促进纤溶酶原激活和宿主细胞侵袭。支原体α-烯醇化酶也是一种纤溶酶原结合蛋白。分子间相互作用 肺炎支原体烯醇化酶与宿主纤溶酶原的相互作用将有助于探索病原体-宿主相互作用。为了鉴定M. pneumoniae烯醇化酶，进行同源建模和对接研究以获得M.肺炎烯醇化酶-纤溶酶原复合物。对改进后的模型进行了进一步验证 通过标准方法。分子对接揭示了eLys 70-pgTyr 50、eAsn 165-pgThr 66、eAla 168-pgGlu 21、eAsp 17-pgLys 70和eAsn 213-pgPro 68/pgAsn 69的氢键。观察到可及表面积（阿萨）的大幅下降，并与氢键模式一致。这些发现提供了一个详细的预测，在蛋白质-蛋白质界面相互作用的关键残基。 我们的理论预测与已知的生化数据是一致的。预测的相互作用复合物可以在理解结构的见解，这是必要的病原体和主机组件的相互作用有很大帮助。M的能力。肺炎克雷伯菌烯醇化酶结合纤溶酶原可能在该病原体入侵宿主中起重要作用。
Alpha (α)-enolase (e), a glycolytic enzyme, has an alternative role as a surface receptor of several bacteria mediating plasminogen (pg) binding. It is also recognized as a virulence factor of some pathogenic bacteria facilitating plasminogen activation and host cell invasion. A mycoplasmal α-enolase is also a plasminogen binding protein. Molecular interactions of enolase from Mycoplasma pneumoniae with host plasminogen would be useful for exploring the pathogen-host interaction. In an attempt to identify plasminogen binding sites of M. pneumoniae enolase, homology modeling and docking studies were conducted to obtain modeled structures of the M. pneumoniae enolase-plasminogen complex. The refined model was validated further by standard methods. Molecular docking revealed hydrogen bonding of eLys70-pgTyr50, eAsn165-pgThr66, eAla168-pgGlu21, eAsp17-pgLys70, and eAsn213-pgPro68/pgAsn69. Substantial decreases in accessible surface area (ASA) were observed and in concurrence with hydrogen bond pattern. These findings provide a detailed prediction of key residues that interact at the protein-protein interface. Our theoretical prediction is consistent with known biochemical data. The predicted interaction complex can be of great assistance in understanding structural insights, which is necessary to pathogen and host-component interaction. The ability of M. pneumoniae enolase to bind plasminogen may be indicative of an important role in invasion of this pathogen to host.