1u8t

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|PDB= 1u8t |SIZE=350|CAPTION= <scene name='initialview01'>1u8t</scene>, resolution 1.50&Aring;
|PDB= 1u8t |SIZE=350|CAPTION= <scene name='initialview01'>1u8t</scene>, resolution 1.50&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= cheY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= cheY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=[[3chy|3CHY]], [[1fqw|1FQW]], [[1f4v|1F4V]], [[1ehc|1EHC]], [[5chy|5CHY]], [[1d4z|1D4Z]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1u8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u8t OCA], [http://www.ebi.ac.uk/pdbsum/1u8t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1u8t RCSB]</span>
}}
}}
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[[Category: Quillin, M L.]]
[[Category: Quillin, M L.]]
[[Category: Westbrook, E M.]]
[[Category: Westbrook, E M.]]
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[[Category: SO4]]
 
[[Category: (beta/alpha)5]]
[[Category: (beta/alpha)5]]
[[Category: chey]]
[[Category: chey]]
[[Category: flim]]
[[Category: flim]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:28:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:06:55 2008''

Revision as of 21:06, 30 March 2008


PDB ID 1u8t

Drag the structure with the mouse to rotate
, resolution 1.50Å
Ligands: ,
Gene: cheY (Escherichia coli)
Related: 3CHY, 1FQW, 1F4V, 1EHC, 5CHY, 1D4Z


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of CheY D13K Y106W alone and in complex with a FliM peptide


Overview

CheY is a member of the response regulator protein superfamily that controls the chemotactic swimming response of motile bacteria. The CheY double mutant D13K Y106W (CheY**) is resistant to phosphorylation, yet is a highly effective mimic of phosphorylated CheY in vivo and in vitro. The conformational attributes of this protein that enable it to signal in a phosphorylation-independent manner are unknown. We have solved the crystal structure of selenomethionine-substituted CheY** in the presence of its target, a peptide (FliM16) derived from the flagellar motor switch, FliM, to 1.5A resolution with an R-factor of 19.6%. The asymmetric unit contains four CheY** molecules, two with FliM16 bound, and two without. The two CheY** molecules in the asymmetric unit that are bound to FliM16 adopt a conformation similar to BeF3- -activated wild-type CheY, and also bind FliM16 in a nearly identical manner. The CheY** molecules that do not bind FliM16 are found in a conformation similar to unphosphorylated wild-type CheY, suggesting that the active phenotype of this mutant is enabled by a facile interconversion between the active and inactive conformations. Finally, we propose a ligand-binding model for CheY and CheY**, in which Ile95 changes conformation in a Tyr/Trp106-dependent manner to accommodate FliM.

About this Structure

1U8T is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the constitutively active double mutant CheYD13K Y106W alone and in complex with a FliM peptide., Dyer CM, Quillin ML, Campos A, Lu J, McEvoy MM, Hausrath AC, Westbrook EM, Matsumura P, Matthews BW, Dahlquist FW, J Mol Biol. 2004 Sep 24;342(4):1325-35. PMID:15351654

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