6chy
From Proteopedia
(New page: 200px<br /><applet load="6chy" size="450" color="white" frame="true" align="right" spinBox="true" caption="6chy, resolution 2.33Å" /> '''STRUCTURE OF CHEMOTA...) |
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| - | [[Image:6chy.gif|left|200px]]<br /><applet load="6chy" size=" | + | [[Image:6chy.gif|left|200px]]<br /><applet load="6chy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="6chy, resolution 2.33Å" /> | caption="6chy, resolution 2.33Å" /> | ||
'''STRUCTURE OF CHEMOTAXIS PROTEIN CHEY'''<br /> | '''STRUCTURE OF CHEMOTAXIS PROTEIN CHEY'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Position 106 in CheY is highly conserved as an aromatic residue in the | + | Position 106 in CheY is highly conserved as an aromatic residue in the response regulator superfamily. In the structure of the wild-type, apo-CheY, Tyr106 is a rotamer whose electron density is observed in both the inside and the outside positions. In the structure of the T87I mutant of CheY, the threonine to isoleucine change at position 87 causes the side chain of Tyr106 to be exclusively restricted to the outside position. In this report we demonstrate that the T87I mutation causes cells to be smooth swimming and non-chemotactic. We also show that another CheY mutant, Y106W, causes cells to be more tumbly than wild-type CheY, and impairs chemotaxis. In the structure of Y106W, the side chain of Trp106 stays exclusively in the inside position. Furthermore, a T87I/Y106W double mutant, which confers the same phenotype as T87I, restricts the side chain of Trp106 to the outside position. The results from these behavioral and structural studies indicate that the rotameric nature of the Tyr106 residue is involved in activation of the CheY molecule. Specifically, CheY's signaling ability correlates with the conformational heterogeneity of the Tyr106 side chain. Our data also suggest that these mutations affect the signal at an event subsequent to phosphorylation. |
==About this Structure== | ==About this Structure== | ||
| - | 6CHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 6CHY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CHY OCA]. |
==Reference== | ==Reference== | ||
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[[Category: two-component systems]] | [[Category: two-component systems]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:16:10 2008'' |
Revision as of 17:16, 21 February 2008
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STRUCTURE OF CHEMOTAXIS PROTEIN CHEY
Overview
Position 106 in CheY is highly conserved as an aromatic residue in the response regulator superfamily. In the structure of the wild-type, apo-CheY, Tyr106 is a rotamer whose electron density is observed in both the inside and the outside positions. In the structure of the T87I mutant of CheY, the threonine to isoleucine change at position 87 causes the side chain of Tyr106 to be exclusively restricted to the outside position. In this report we demonstrate that the T87I mutation causes cells to be smooth swimming and non-chemotactic. We also show that another CheY mutant, Y106W, causes cells to be more tumbly than wild-type CheY, and impairs chemotaxis. In the structure of Y106W, the side chain of Trp106 stays exclusively in the inside position. Furthermore, a T87I/Y106W double mutant, which confers the same phenotype as T87I, restricts the side chain of Trp106 to the outside position. The results from these behavioral and structural studies indicate that the rotameric nature of the Tyr106 residue is involved in activation of the CheY molecule. Specifically, CheY's signaling ability correlates with the conformational heterogeneity of the Tyr106 side chain. Our data also suggest that these mutations affect the signal at an event subsequent to phosphorylation.
About this Structure
6CHY is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106., Zhu X, Rebello J, Matsumura P, Volz K, J Biol Chem. 1997 Feb 21;272(8):5000-6. PMID:9030562
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