Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module
Sun, JP; Zhang, JH; Wu, FM; Xu, C; Li, SJ; Zhao, W; Wu, ZY; Wu, JH; Zhou, CZ; Shi, YY
刊名BIOCHEMISTRY
2005
卷号44期号:24页码:8801-8809
通讯作者Univ Sci & Technol China, Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China ; Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Anhui, Peoples R China ; Chinese Acad Sci, Beijing Synchrotron Radiat Facil, Inst High Energy Phys, Beijing 100039, Peoples R China
英文摘要Kti11p is a small, highly conserved CSL zinc finger-containing protein found in many eukaryotes. It was first identified as one of the factors required for maintaining the sensitivity of Saccharomyces cerevisiae to Kluyveromyces lactis zymocin. Then, it was found to be identical to Dph3, a protein required for diphthamide biosynthesis on eEF-2, the target of diphtheria toxin and Pseudomonas exotoxin A, in both yeast and higher eukaryotes. Furthermore, Kti11p/Dph3 was found to physically interact with core-Elongator, ribosomal proteins, eEF-2, two other proteins required for diphthamide modification on eEF-2, and De1GEF. Here, we determined the solution structure of Kti11p using NMR, providing the first structure of the CSL-class zinc-binding protein family. We present the first experimental evidence that Kti11p can bind a single Zn2+ ion by its four conserved cysteine residues. The major structure of Kti11p comprises a beta sandwich as well as an a helix. Moreover, a structure-based similarity search suggests that it represents a novel structure and may define a new family of the zinc ribbon fold group. Therefore, our work provides a molecular basis for further understanding the multiple functions of Kti11p/Dph3 in different biological processes.
学科主题Biochemistry & Molecular Biology
类目[WOS]Biochemistry & Molecular Biology
研究领域[WOS]Biochemistry & Molecular Biology
原文出处SCI
语种英语
WOS记录号WOS:000229994900025
内容类型期刊论文
源URL[http://ir.ihep.ac.cn/handle/311005/240152]  
专题高能物理研究所_多学科研究中心
高能物理研究所_实验物理中心
高能物理研究所_加速器中心
中国科学院高能物理研究所_大装置管理中心
作者单位中国科学院高能物理研究所
推荐引用方式
GB/T 7714
Sun, JP,Zhang, JH,Wu, FM,et al. Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module[J]. BIOCHEMISTRY,2005,44(24):8801-8809.
APA Sun, JP.,Zhang, JH.,Wu, FM.,Xu, C.,Li, SJ.,...&吴自玉.(2005).Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module.BIOCHEMISTRY,44(24),8801-8809.
MLA Sun, JP,et al."Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module".BIOCHEMISTRY 44.24(2005):8801-8809.
个性服务
查看访问统计
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。


©版权所有 ©2017 CSpace - Powered by CSpace