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金黄色葡萄球菌 MepB 的结构特征分析揭示了其与内切核酸酶的同源性。

Structural characterization of MepB from Staphylococcus aureus reveals homology to endonucleases.

机构信息

Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, Virginia.

出版信息

Protein Sci. 2014 May;23(5):594-602. doi: 10.1002/pro.2438. Epub 2014 Mar 11.

Abstract

The MepRAB operon in Staphylococcus aureus has been identified to play a role in drug resistance. Although the functions of MepA and MepR are known, little information is available on the function of MepB. Here we report the X-ray structure of MepB to 2.1 Å revealing its structural similarity to the PD-(D/E)XK family of endonucleases. We further show that MepB binds DNA and RNA, with a higher affinity towards RNA and single stranded DNA than towards double stranded DNA. Notably, the PD-(D/E)XK catalytic active site residues are not conserved in MepB. MepB's association with a drug resistance operon suggests that it plays a role in responding to antimicrobials. This role is likely carried out through MepB's interactions with nucleic acids.

摘要

金黄色葡萄球菌中的 MepRAB 操纵子已被确定在耐药性中发挥作用。尽管已知 MepA 和 MepR 的功能,但关于 MepB 的功能知之甚少。在这里,我们报道了 MepB 的 X 射线结构,分辨率为 2.1Å,揭示了其与 PD-(D/E)XK 家族内切酶的结构相似性。我们进一步表明,MepB 结合 DNA 和 RNA,与 RNA 和单链 DNA 的亲和力高于双链 DNA。值得注意的是,MepB 中没有保守的 PD-(D/E)XK 催化活性位点残基。MepB 与耐药性操纵子的关联表明它在对抗微生物药物的反应中发挥作用。这种作用可能是通过 MepB 与核酸的相互作用来实现的。

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