Myroilysin Is a New Bacterial Member of the M12A Family of Metzincin Metallopeptidases and Is Activated by a Cysteine Switch Mechanism
Xu, DQ; Zhou, JL; Lou, XD; He, JH; Ran, TT; Wang, WW
2017
发表期刊JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN0021-9258
卷号292期号:13页码:5195-5206
文章类型期刊论文
摘要Proteases play important roles in all living organisms and also have important industrial applications. Family M12A metalloproteases, mainly found throughout the animal kingdom, belong to the metzincin protease family and are synthesized as inactive precursors. So far, only flavastacin and myroilysin, isolated from bacteria, were reported to be M12A proteases, whereas the classification of myroilysin is still unclear due to the lack of structural information. Here, we report the crystal structures of pro-myroilysin from bacterium Myroides sp. cslb8. The catalytic zinc ion of pro-myroilysin, at the bottom of a deep active site, is coordinated by three histidine residues in the conserved motif HEXXHXXGXXH; the cysteine residue in the propeptide coordinates the catalytic zinc ion and inhibits myroilysin activity. Structure comparisons revealed that myroilysin shares high similarity with the members of the M12A, M10A, and M10B families of metalloproteases. However, a unique "cap" structure tops the active site cleft in the structure of pro-myroilysin, and this "cap" structure does not exist in the above structure-reported subfamilies. Further structure-based sequence analysis revealed that myroilysin appears to belong to the M12A family, but pro-myroilysin uses a "cysteine switch" activation mechanism with a unique segment, including the conserved cysteine residue, whereas other reported M12A family proteases use an "aspartate switch" activation mechanism. Thus, our results suggest that myroilysin is a new bacterial member of the M12A family with an exceptional cysteine switch activation mechanism. Our results shed new light on the classification of the M12A family and may suggest a divergent evolution of the M12 family.
DOI10.1074/jbc.M116.758110
收录类别SCI
语种英语
WOS记录号WOS:000397875500004
引用统计
被引频次:2[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.sinap.ac.cn/handle/331007/27390
专题中科院上海应用物理研究所2011-2018年
推荐引用方式
GB/T 7714
Xu, DQ,Zhou, JL,Lou, XD,et al. Myroilysin Is a New Bacterial Member of the M12A Family of Metzincin Metallopeptidases and Is Activated by a Cysteine Switch Mechanism[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2017,292(13):5195-5206.
APA Xu, DQ,Zhou, JL,Lou, XD,He, JH,Ran, TT,&Wang, WW.(2017).Myroilysin Is a New Bacterial Member of the M12A Family of Metzincin Metallopeptidases and Is Activated by a Cysteine Switch Mechanism.JOURNAL OF BIOLOGICAL CHEMISTRY,292(13),5195-5206.
MLA Xu, DQ,et al."Myroilysin Is a New Bacterial Member of the M12A Family of Metzincin Metallopeptidases and Is Activated by a Cysteine Switch Mechanism".JOURNAL OF BIOLOGICAL CHEMISTRY 292.13(2017):5195-5206.
条目包含的文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
Myroilysin Is a New (1006KB)期刊论文作者接受稿开放获取CC BY-NC-SA请求全文
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Xu, DQ]的文章
[Zhou, JL]的文章
[Lou, XD]的文章
百度学术
百度学术中相似的文章
[Xu, DQ]的文章
[Zhou, JL]的文章
[Lou, XD]的文章
必应学术
必应学术中相似的文章
[Xu, DQ]的文章
[Zhou, JL]的文章
[Lou, XD]的文章
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。