1yop

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Revision as of 04:49, 21 November 2007

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The solution structure of Kti11p

Overview

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.

About this Structure

1YOP is a Single protein structure of sequence from Saccharomyces cerevisiae with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Solution structure of Kti11p from Saccharomyces cerevisiae reveals a novel zinc-binding module., Sun J, Zhang J, Wu F, Xu C, Li S, Zhao W, Wu Z, Wu J, Zhou CZ, Shi Y, Biochemistry. 2005 Jun 21;44(24):8801-9. PMID:15952786

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