Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module.

@article{Sun2005SolutionSO,
  title={Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module.},
  author={J. Sun and Jiahai Zhang and Fangming Wu and Chao Xu and Shujun Li and Wei Zhao and Ziyu Wu and Jihui Wu and Cong-Zhao Zhou and Yunyu Shi},
  journal={Biochemistry},
  year={2005},
  volume={44 24},
  pages={
          8801-9
        }
}
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… Expand
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3D local structure around Zn in Kti11p as a representative Zn-(Cys)4 motif as obtained by MXAN.
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