4tmy
From Proteopedia
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==Overview== | ==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, . | + | 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== | ==About this Structure== | ||
| - | 4TMY is a | + | 4TMY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Sites: ACA and ACB. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4TMY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:59:44 2007'' |
Revision as of 11:54, 5 November 2007
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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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