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- PDB-1glf: CRYSTAL STRUCTURES OF ESCHERICHIA COLI GLYCEROL KINASE AND THE MU... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1glf | ||||||
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Title | CRYSTAL STRUCTURES OF ESCHERICHIA COLI GLYCEROL KINASE AND THE MUTANT A65T IN AN INACTIVE TETRAMER: CONFORMATIONAL CHANGES AND IMPLICATIONS FOR ALLOSTERIC REGULATION | ||||||
![]() | PROTEIN (GLYCEROL KINASE) | ||||||
![]() | TRANSFERASE / ALLOSTERY / COOPERATIVITY / GLYCEROL KINASE | ||||||
Function / homology | ![]() glycerol kinase / glycerol-3-phosphate biosynthetic process / glycerol kinase activity / glycerol metabolic process / glycerol catabolic process / triglyceride metabolic process / phosphorylation / DNA damage response / zinc ion binding / ATP binding ...glycerol kinase / glycerol-3-phosphate biosynthetic process / glycerol kinase activity / glycerol metabolic process / glycerol catabolic process / triglyceride metabolic process / phosphorylation / DNA damage response / zinc ion binding / ATP binding / identical protein binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Feese, M.D. / Faber, H.R. / Bystrom, C.E. / Pettigrew, D.W. / Remington, S.J. | ||||||
![]() | ![]() Title: Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation. Authors: Feese, M.D. / Faber, H.R. / Bystrom, C.E. / Pettigrew, D.W. / Remington, S.J. #1: ![]() Title: A Single Amino Acid Change in Escherichia Coli Glycerol Kinase Abolishes Glucose Control of Glycerol Utilization in Vivo Authors: Pettigrew, D.W. / Liu, W.Z. / Holmes, C. / Meadow, N.D. / Roseman, S. #2: ![]() Title: Cation Promoted Association (Cpa) of a Regulatory and Target Protein is Controlled by Protein Phosphorylation Authors: Feese, M.D. / Pettigrew, D.W. / Meadow, N.D. / Roseman, S. / Remington, S.J. #3: ![]() Title: Escherichia Coli Glycerol Kinase: Role of a Tetramer Interface in Regulation by Fructose-1,6-Bisphosphate and Phoshotransferase System Regulatory Protein Iiiglc Authors: Liu, W.Z. / Faber, H.R. / Feese, M.D. / Remington, S.J. / Pettigrew, D.W. #4: ![]() Title: Structure of the Regulatory Complex of Escherichia Coli III==Glc== with Glycerol Kinase Authors: Hurley, J.H. / Faber, H.R. / Worthylake, D. / Meadow, N.D. / Roseman, S. / Pettigrew, D.W. / Remington, S.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 400.5 KB | Display | ![]() |
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PDB format | ![]() | 321.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 101.8 KB | Display | |
Data in CIF | ![]() | 135.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1bu6C ![]() 1glaS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 56162.352 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: GLYCEROL ADENOSINE DIPHOSPHATE ORTHOPHOSPHATE / Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | ChemComp-ADP / #4: Chemical | ChemComp-GOL / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.6 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.50 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: Faber, H.R., (1989) J. Mol. Biol., 207, 637. / PH range low: 7 / PH range high: 6.5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: SDMS / Detector: AREA DETECTOR / Date: Aug 1, 1990 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.62→20 Å / Num. obs: 58942 / % possible obs: 84 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Biso Wilson estimate: 20.9 Å2 / Rmerge(I) obs: 0.076 |
Reflection | *PLUS Highest resolution: 2.62 Å / Lowest resolution: 20 Å / Observed criterion σ(I): 2 / Redundancy: 3 % / Num. measured all: 190143 / Biso Wilson estimate: 20.9 Å2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1GLA Resolution: 2.62→20 Å / Isotropic thermal model: TNT BCORREL V1.0 / σ(F): 0 / Stereochemistry target values: TNT PROTGEO Details: BSOL AND KSOL SET BY USER GLYCEROL KINASE EXISTS AT PHYSIOLOGICAL CONCENTRATIONS IN AN EQUILIBRIUM BETWEEN FUNCTIONAL DIMERS AND TETRAMERS. THE CRYSTAL ASYMMETRIC UNIT CONTAINS A TETRAMER OF ...Details: BSOL AND KSOL SET BY USER GLYCEROL KINASE EXISTS AT PHYSIOLOGICAL CONCENTRATIONS IN AN EQUILIBRIUM BETWEEN FUNCTIONAL DIMERS AND TETRAMERS. THE CRYSTAL ASYMMETRIC UNIT CONTAINS A TETRAMER OF GLYCEROL KINASE WITH NEARLY EXACT 222 POINT-GROUP SYMMETRY, UNLIKE THE PREVIOUSLY SUBMITTED GLYCEROL KINASE - FACTOR IIIGLC COMPLEX IN WHICH THE 222 POINT GROUP SYMMETRY WAS CRYSTALLOGRAPHICALLY ENFORCED
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Solvent computation | Solvent model: TNT SOLVENT MODELING / Bsol: 300 Å2 / ksol: 0.8 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.62→20 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Version: 5F-6 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.146 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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