1u0s: Difference between revisions
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[[Image:1u0s.gif|left|200px]] | [[Image:1u0s.gif|left|200px]] | ||
'''Chemotaxis kinase CheA P2 domain in complex with response regulator CheY from the thermophile thermotoga maritima''' | {{Structure | ||
|PDB= 1u0s |SIZE=350|CAPTION= <scene name='initialview01'>1u0s</scene>, resolution 1.9Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= chey ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]), chea ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | |||
}} | |||
'''Chemotaxis kinase CheA P2 domain in complex with response regulator CheY from the thermophile thermotoga maritima''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1U0S is a [ | 1U0S is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U0S OCA]. | ||
==Reference== | ==Reference== | ||
In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved., Park SY, Beel BD, Simon MI, Bilwes AM, Crane BR, Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11646-51. Epub 2004 Aug 2. PMID:[http:// | In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved., Park SY, Beel BD, Simon MI, Bilwes AM, Crane BR, Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11646-51. Epub 2004 Aug 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15289606 15289606] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
[[Category: signaling complex]] | [[Category: signaling complex]] | ||
[[Category: transient complex of thermostable | [[Category: transient complex of thermostable protein]] | ||
[[Category: transient interaction]] | [[Category: transient interaction]] | ||
''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 14:25:48 2008'' | ||
Revision as of 15:25, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Gene: | chey (Thermotoga maritima), chea (Thermotoga maritima) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Chemotaxis kinase CheA P2 domain in complex with response regulator CheY from the thermophile thermotoga maritima
OverviewOverview
Although interfaces mediating protein-protein interactions are thought to be under strong evolutionary constraints, binding of the chemotaxis histidine kinase CheA to its phosphorylation target CheY suggests otherwise. The structure of Thermotoga maritima CheA domain P2 in complex with CheY reveals a different association than that observed for the same Escherichia coli proteins. Similar regions of CheY bind CheA P2 in the two systems, but the CheA P2 domains differ by an approximately 90 degrees rotation. CheA binds CheY with identical affinity in T. maritima and E. coli at the vastly different temperatures where the respective organisms live. Distinct sets of P2 residues mediate CheY binding in the two complexes; conservation patterns of these residues in CheA and compensations in CheY delineate two families of prokaryotic chemotaxis systems. A protein complex that has the same components and general function in different organisms, but an altered structure, indicates unanticipated complexity in the evolution of protein-protein interactions and cautions against extrapolating structural data from homologs.
About this StructureAbout this Structure
1U0S is a Protein complex structure of sequences from Thermotoga maritima. Full crystallographic information is available from OCA.
ReferenceReference
In different organisms, the mode of interaction between two signaling proteins is not necessarily conserved., Park SY, Beel BD, Simon MI, Bilwes AM, Crane BR, Proc Natl Acad Sci U S A. 2004 Aug 10;101(32):11646-51. Epub 2004 Aug 2. PMID:15289606
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