3chy
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:3chy.gif|left|200px]] | + | [[Image:3chy.gif|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF ESCHERICHIA COLI CHEY REFINED AT 1.7-ANGSTROM RESOLUTION''' | + | {{Structure |
| + | |PDB= 3chy |SIZE=350|CAPTION= <scene name='initialview01'>3chy</scene>, resolution 1.66Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF ESCHERICHIA COLI CHEY REFINED AT 1.7-ANGSTROM RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 3CHY is a [ | + | 3CHY 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=3CHY OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of Escherichia coli CheY refined at 1.7-A resolution., Volz K, Matsumura P, J Biol Chem. 1991 Aug 15;266(23):15511-9. PMID:[http:// | + | Crystal structure of Escherichia coli CheY refined at 1.7-A resolution., Volz K, Matsumura P, J Biol Chem. 1991 Aug 15;266(23):15511-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1869568 1869568] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 18: | Line 27: | ||
[[Category: signal transduction protein]] | [[Category: signal transduction 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 19:04:03 2008'' |
Revision as of 17:04, 20 March 2008
| |||||||
| , resolution 1.66Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ESCHERICHIA COLI CHEY REFINED AT 1.7-ANGSTROM RESOLUTION
Overview
The three-dimensional structure of wild-type CheY from Escherichia coli has been refined by stereochemically restrained least squares minimization to a crystallographic R-factor of 15.1% at 1.7-A resolution. The structure contains 1165 atoms, including all atoms of the protein, 147 water molecules, and three sulfate ions. The final model has root mean square deviations of 0.018 and 0.049 A from idealized bond lengths and angle distances, respectively. Seven amino acid side chains have been modeled in dual conformations. CheY folds as a compact (beta/alpha)5 globular protein, with the phosphorylation region contained in a cavity on one face of the molecule. This active site area is bordered by the carboxyl termini of the three central beta-strands, by alpha 1, and by the loop connecting beta 5 to alpha 5. The Lys-109 side chain of this loop extends into the active site by virtue of its cis peptide bond conformation preceding Pro-110. The epsilon-amino group of Lys-109 is in close bonding contact with the carboxyl group of Asp-57, the residue that is phosphorylated in the activation process of CheY. The details of the hydrogen bonding network in the phosphorylation region indicate that structural rearrangements must accompany the phosphorylation of Asp-57.
About this Structure
3CHY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of Escherichia coli CheY refined at 1.7-A resolution., Volz K, Matsumura P, J Biol Chem. 1991 Aug 15;266(23):15511-9. PMID:1869568
Page seeded by OCA on Thu Mar 20 19:04:03 2008
