1a0o
From Proteopedia
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| - | [[Image:1a0o.gif|left|200px]] | + | [[Image:1a0o.gif|left|200px]] |
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| - | '''CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY''' | + | {{Structure |
| + | |PDB= 1a0o |SIZE=350|CAPTION= <scene name='initialview01'>1a0o</scene>, resolution 2.95Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1A0O is a [ | + | 1A0O 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=1A0O OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY., Welch M, Chinardet N, Mourey L, Birck C, Samama JP, Nat Struct Biol. 1998 Jan;5(1):25-9. PMID:[http:// | + | Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY., Welch M, Chinardet N, Mourey L, Birck C, Samama JP, Nat Struct Biol. 1998 Jan;5(1):25-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9437425 9437425] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: two-component system]] | [[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 09:51:17 2008'' |
Revision as of 07:51, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHEY-BINDING DOMAIN OF CHEA IN COMPLEX WITH CHEY
Overview
Bacterial adaptation to the environment is accomplished through the coordinated activation of specific sensory receptors and signal processing proteins. Among the best characterized of these pathways are those which employ the two-component paradigm. In these systems, signal transmission is mediated by Mg(2+)-dependent phospho-relay reactions between histidine auto-kinases and phospho-accepting receiver domains in response-regulator proteins. Although this mechanism of activation is common to all response-regulators, detrimental cross-talk between different two-component pathways within the same cell is minimized through the use of specific recognition domains. Here, we report the crystal structure, at 2.95 A resolution, of the response regulator of bacterial chemotaxis, CheY, bound to the recognition domain from its cognate histidine kinase, CheA. The structure suggests that molecular recognition, in this low affinity complex (KD = 2 microM), may also contribute to the mechanism of CheY activation.
About this Structure
1A0O is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure of the CheY-binding domain of histidine kinase CheA in complex with CheY., Welch M, Chinardet N, Mourey L, Birck C, Samama JP, Nat Struct Biol. 1998 Jan;5(1):25-9. PMID:9437425
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