6chy
From Proteopedia
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| - | [[Image:6chy.gif|left|200px]] | + | [[Image:6chy.gif|left|200px]] |
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| - | '''STRUCTURE OF CHEMOTAXIS PROTEIN CHEY''' | + | {{Structure |
| + | |PDB= 6chy |SIZE=350|CAPTION= <scene name='initialview01'>6chy</scene>, resolution 2.33Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF CHEMOTAXIS PROTEIN CHEY''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 6CHY is a [ | + | 6CHY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CHY OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9030562 9030562] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Zhu, X.]] | [[Category: Zhu, X.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
| - | [[Category: response | + | [[Category: response regulator]] |
[[Category: signal transduction protein]] | [[Category: signal transduction protein]] | ||
| - | [[Category: two-component | + | [[Category: two-component system]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:13:16 2008'' |
Revision as of 17:13, 20 March 2008
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| , resolution 2.33Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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