1e0q

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Revision as of 11:35, 20 November 2007

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MUTANT PEPTIDE FROM THE FIRST N-TERMINAL 17 AMINO-ACID OF UBIQUITIN

Overview

The formation of the N-terminal beta-hairpin of ubiquitin is thought to be, an early event in the folding of this small protein. Previously, we have, shown that a peptide corresponding to residues 1-17 of ubiquitin folds, autonomously and is likely to have a native-like hairpin register. To, investigate the causes of the stability of this fold, we have made, mutations in the amino acids at the apex of the turn. We find that in a, peptide where Thr9 is replaced by Asp, U(1-17)T9D, the native conformation, is stabilized with respect to the wild-type sequence, so much so that we, are able to characterize the structure of the mutant peptide fully by NMR, spectroscopy. The data indicate that U(1-17)T9D peptide does indeed form a, hairpin with a native-like register and a type I turn with a G1, beta-bulge, as in the full-length protein. The reason for the greater, stability of the U(1-17)T9D mutant remains uncertain, but there are, nuclear Overhauser effects between the side chains of Asp9 and Lys 11, which may indicate that a charge-charge interaction between these residues, is responsible.

About this Structure

1E0Q is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Structural characterization of a mutant peptide derived from ubiquitin: implications for protein folding., Zerella R, Chen PY, Evans PA, Raine A, Williams DH, Protein Sci. 2000 Nov;9(11):2142-50. PMID:11152124

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