|Entry||Database: PDB / ID: 1djm|
|Title||SOLUTION STRUCTURE OF BEF3-ACTIVATED CHEY FROM ESCHERICHIA COLI|
|Components||CHEMOTAXIS PROTEIN Y|
|Keywords||SIGNALING PROTEIN / BEFX / CHEY / RESPONSE REGULATOR / CHEMOTAXIS / TWO-COMPONENT|
|Function / homology|
Function and homology information
bacterial-type flagellum basal body, C ring / bacterial-type flagellum rotor complex / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity ...bacterial-type flagellum basal body, C ring / bacterial-type flagellum rotor complex / bacterial-type flagellum-dependent swimming motility / regulation of bacterial-type flagellum-dependent cell motility / aerotaxis / bacterial-type flagellum / regulation of chemotaxis / thermotaxis / internal peptidyl-lysine acetylation / phosphorelay response regulator activity / acetyltransferase activity / protein acetylation / phosphorelay signal transduction system / chemotaxis / magnesium ion binding / signal transduction / cytosol / cytoplasm
Similarity search - Function
Response regulator receiver domain / cheY-homologous receiver domain / Signal transduction response regulator, receiver domain / Response regulatory domain profile. / CheY-like superfamily / Response regulator / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chemotaxis protein CheY / Chemotaxis protein CheY
Similarity search - Component
|Biological species||Escherichia coli (E. coli)|
|Method||SOLUTION NMR / torsion angle dynamics|
|Authors||Cho, H.S. / Lee, S.Y. / Yan, D. / Pan, X. / Parkinson, J.S. / Kustu, S. / Wemmer, D.E. / Pelton, J.G.|
Journal: J.Mol.Biol. / Year: 2000
Title: NMR structure of activated CheY.
Authors: Cho, H.S. / Lee, S.Y. / Yan, D. / Pan, X. / Parkinson, J.S. / Kustu, S. / Wemmer, D.E. / Pelton, J.G.
|Structure viewer||Molecule: |
Downloads & links
A: CHEMOTAXIS PROTEIN Y
|#1: Protein|| |
Mass: 14112.332 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET21 / Production host: Escherichia coli (E. coli) / References: UniProt: P06143, UniProt: P0AE67*PLUS
|Experiment||Method: SOLUTION NMR|
|NMR details||Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY.|
*PLUSMethod: other / Details: NMR
|NMR spectrometer||Type: Bruker AMX / Manufacturer: Bruker / Model: AMX / Field strength: 600 MHz|
|Refinement||Method: torsion angle dynamics / Software ordinal: 1 |
Details: THE STRUCTURES ARE BASED ON A TOTAL OF 972 NON-TRIVIAL NOE RESTRAINTS (213 INTRA RESIDUE, 271 SEQUENTIAL, 238 MEDIUM-RANGE, AND 250 LONG-RANGE). 78 PHI TORSION ANGLE RESTRAINTS AND 17 CHI1 ...Details: THE STRUCTURES ARE BASED ON A TOTAL OF 972 NON-TRIVIAL NOE RESTRAINTS (213 INTRA RESIDUE, 271 SEQUENTIAL, 238 MEDIUM-RANGE, AND 250 LONG-RANGE). 78 PHI TORSION ANGLE RESTRAINTS AND 17 CHI1 RESTRAINTS WERE USED. 47 HYDROGEN BONDS ( 94 UPPER AND LOWER DISTANCE RESTRAINTS) WERE USED IN LATER STAGES OF REFINEMENT.
|NMR representative||Selection criteria: fewest violations|
|NMR ensemble||Conformer selection criteria: structures with the least restraint violations|
Conformers calculated total number: 60 / Conformers submitted total number: 27
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