4tmy

From Proteopedia

Revision as of 16:44, 5 November 2007

CHEY FROM THERMOTOGA MARITIMA (MG-IV)

Overview

The crystal structure of CheY protein from Thermotoga maritima has been, determined in four crystal forms with and without Mg++ bound, at up to 1.9, A resolution. Structural comparisons with CheY from Escherichia coli shows, substantial similarity in their folds, with some concerted changes, propagating away from the active site that suggest how phosphorylated, CheY, a signal transduction protein in bacterial chemotaxis, is recognized, by its targets. A highly conserved segment of the protein (the "y-turn, loop," residues 55-61), previously suggested to be a rigid recognition, determinant, is for the first time seen in two alternative conformations, in the different crystal structures. Although CheY from Thermotoga has, much higher thermal stability than its mesophilic counterparts, comparison, of structural features previously proposed to enhance thermostability such, as hydrogen bonds, ion pairs, compactness, and hydrophobic surface burial, would not suggest it to be so.

About this Structure

4TMY is a Single protein structure of sequence from Thermotoga maritima with MG as ligand. Structure known Active Sites: ACA and ACB. Full crystallographic information is available from OCA.

Reference

Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability., Usher KC, de la Cruz AF, Dahlquist FW, Swanson RV, Simon MI, Remington SJ, Protein Sci. 1998 Feb;7(2):403-12. PMID:9521117

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