1d4z
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1d4z.jpg|left|200px]] | + | [[Image:1d4z.jpg|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF CHEY-95IV, A HYPERACTIVE CHEY MUTANT''' | + | {{Structure |
| + | |PDB= 1d4z |SIZE=350|CAPTION= <scene name='initialview01'>1d4z</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF CHEY-95IV, A HYPERACTIVE CHEY MUTANT''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1D4Z is a [ | + | 1D4Z 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=1D4Z OCA]. |
==Reference== | ==Reference== | ||
| - | Correlated switch binding and signaling in bacterial chemotaxis., Schuster M, Zhao R, Bourret RB, Collins EJ, J Biol Chem. 2000 Jun 30;275(26):19752-8. PMID:[http:// | + | Correlated switch binding and signaling in bacterial chemotaxis., Schuster M, Zhao R, Bourret RB, Collins EJ, J Biol Chem. 2000 Jun 30;275(26):19752-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10748173 10748173] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 22: | Line 31: | ||
[[Category: signaling protein]] | [[Category: signaling protein]] | ||
| - | ''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 10:32:57 2008'' |
Revision as of 08:32, 20 March 2008
| |||||||
| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF CHEY-95IV, A HYPERACTIVE CHEY MUTANT
Overview
In Escherichia coli, swimming behavior is mediated by the phosphorylation state of the response regulator CheY. In its active, phosphorylated form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor, which induces a change from counterclockwise to clockwise flagellar rotation. When Ile(95) of CheY is replaced by a valine, increased clockwise rotation correlates with enhanced binding to FliM. A possible explanation for the hyperactivity of this mutant is that residue 95 affects the conformation of nearby residues that potentially interact with FliM. In order to assess this possibility directly, the crystal structure of CheY95IV was determined. We found that CheY95IV is structurally almost indistinguishable from wild-type CheY. Several other mutants with substitutions at position 95 were characterized to establish the structural requirements for switch binding and clockwise signaling at this position and to investigate a general relationship between the two properties. The various rotational phenotypes of these mutants can be explained solely by the amount of phosphorylated CheY bound to the switch, which was inferred from the phosphorylation properties of the mutant CheY proteins and their binding affinities to FliM. Combined genetic, biochemical, and crystallographic results suggest that residue 95 itself is critical in mediating the surface complementarity between CheY and FliM.
About this Structure
1D4Z is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Correlated switch binding and signaling in bacterial chemotaxis., Schuster M, Zhao R, Bourret RB, Collins EJ, J Biol Chem. 2000 Jun 30;275(26):19752-8. PMID:10748173
Page seeded by OCA on Thu Mar 20 10:32:57 2008
