1YOP

The solution structure of Kti11p

Summary for 1YOP

• Entry DOI: 10.2210/pdb1yop/pdb
• Descriptor: Kti11p, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger, metal binding protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: Q3E840
• Total number of polymer chains: 1
• Total formula weight: 9524.96

Authors

Sun, J.,Zhang, J.,Wu, F.,Xu, C.,Li, S.,Zhao, W.,Wu, Z.,Wu, J.,Zhou, C.-Z.,Shi, Y. (deposition date: 2005-01-28, release date: 2005-04-05, Last modification date: 2024-05-29)

Primary citation

Sun, J.,Zhang, J.,Wu, F.,Xu, C.,Li, S.,Zhao, W.,Wu, Z.,Wu, J.,Zhou, C.Z.,Shi, Y.
Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module.
Biochemistry, 44:8801-8809, 2005

PubMed Abstract: 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 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 experimental evidence that Kti11p can bind a single Zn(2+) ion by its four conserved cysteine residues. The major structure of Kti11p comprises a beta sandwich as well as an alpha 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.

PubMed: 15952786
DOI: 10.1021/bi0504714

Experimental method

SOLUTION NMR