1eay
From Proteopedia
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| - | [[Image:1eay.gif|left|200px]] | + | [[Image:1eay.gif|left|200px]] |
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| - | '''CHEY-BINDING (P2) DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM ESCHERICHIA COLI''' | + | {{Structure |
| + | |PDB= 1eay |SIZE=350|CAPTION= <scene name='initialview01'>1eay</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CHEY-BINDING (P2) DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM ESCHERICHIA COLI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1EAY is a [ | + | 1EAY is a [[Protein complex]] structure of sequences 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=1EAY OCA]. |
==Reference== | ==Reference== | ||
| - | Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway., McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW, Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7333-8. PMID:[http:// | + | Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway., McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW, Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7333-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9636149 9636149] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: signal transduction complex]] | [[Category: signal transduction complex]] | ||
| - | ''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 10:52:51 2008'' |
Revision as of 08:52, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHEY-BINDING (P2) DOMAIN OF CHEA IN COMPLEX WITH CHEY FROM ESCHERICHIA COLI
Overview
The crystal structure at 2.0-A resolution of the complex of the Escherichia coli chemotaxis response regulator CheY and the phosphoacceptor-binding domain (P2) of the kinase CheA is presented. The binding interface involves the fourth and fifth helices and fifth beta-strand of CheY and both helices of P2. Surprisingly, the two heterodimers in the asymmetric unit have two different binding modes involving the same interface, suggesting some flexibility in the binding regions. Significant conformational changes have occurred in CheY compared with previously determined unbound structures. The active site of CheY is exposed by the binding of the kinase domain, possibly to enhance phosphotransfer from CheA to CheY. The conformational changes upon complex formation as well as the observation that there are two different binding modes suggest that the plasticity of CheY is an essential feature of response regulator function.
About this Structure
1EAY is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway., McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW, Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7333-8. PMID:9636149
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