Solution Structure of Kti11p from Saccharomyces cerevisiae Reveals a Novel Zinc-Binding Module
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- 作者：Jianping Sun ; Jiahai Zhang ; Fangming Wu ; Chao Xu ; Shujun Li ; Wei Zhao ; Ziyu Wu ; Jihui Wu ; Cong-Zhao Zhou ; and Yunyu Shi
- 刊名：Biochemistry
- 出版年：2005
- 出版时间：June 21, 2005
- 年：2005
- 卷：44
- 期：24
- 页码：8801 - 8809
- 全文大小：674K
- 年卷期：v.44,no.24(June 21, 2005)
- ISSN：1520-4995
文摘
Kti11p is a small, highly conserved CSL zinc finger-containing protein found in manyeukaryotes. It was first identified as one of the factors required for maintaining the sensitivity ofSaccharomyces 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 Pseudomonasexotoxin A, in both yeast and higher eukaryotes. Furthermore, Kti11p/Dph3 was found to physicallyinteract with core-Elongator, ribosomal proteins, eEF-2, two other proteins required for diphthamidemodification on eEF-2, and DelGEF. 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 experimentalevidence that Kti11p can bind a single Zn2+ ion by its four conserved cysteine residues. The major structureof Kti11p comprises a 
sandwich as well as an 
helix. Moreover, a structure-based similarity searchsuggests 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.
sandwich as well as an helix. Moreover, a structure-based similarity searchsuggests 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.