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- PDB-4ox2: I45T cytosolic phosphoenolpyruvate carboxykinase in complex with ... -

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Basic information

Entry
Database: PDB / ID: 4ox2
TitleI45T cytosolic phosphoenolpyruvate carboxykinase in complex with beta-sulfopyruvate and GTP
ComponentsPhosphoenolpyruvate carboxykinase, cytosolic [GTP]
KeywordsLYASE / kinase / gluconeogenesis
Function / homology
Function and homology information


Gluconeogenesis / phosphoenolpyruvate carboxykinase activity / cellular response to potassium ion starvation / positive regulation of transcription from RNA polymerase II promoter in response to acidic pH / protein serine kinase activity (using GTP as donor) / response to methionine / glycerol biosynthetic process from pyruvate / Transferases; Transferring phosphorus-containing groups; Protein-serine/threonine kinases / propionate catabolic process / cellular response to fructose stimulus ...Gluconeogenesis / phosphoenolpyruvate carboxykinase activity / cellular response to potassium ion starvation / positive regulation of transcription from RNA polymerase II promoter in response to acidic pH / protein serine kinase activity (using GTP as donor) / response to methionine / glycerol biosynthetic process from pyruvate / Transferases; Transferring phosphorus-containing groups; Protein-serine/threonine kinases / propionate catabolic process / cellular response to fructose stimulus / phosphoenolpyruvate carboxykinase (GTP) activity / phosphoenolpyruvate carboxykinase (GTP) / regulation of lipid biosynthetic process / response to interleukin-6 / carboxylic acid binding / oxaloacetate metabolic process / hepatocyte differentiation / positive regulation of memory T cell differentiation / cellular response to glucagon stimulus / nucleoside diphosphate kinase activity / response to starvation / response to lipid / cellular response to interleukin-1 / cellular response to dexamethasone stimulus / cellular response to retinoic acid / gluconeogenesis / response to activity / cellular response to cAMP / response to bacterium / response to insulin / cellular response to glucose stimulus / lipid metabolic process / GDP binding / cellular response to insulin stimulus / glucose metabolic process / glucose homeostasis / cellular response to tumor necrosis factor / cellular response to hypoxia / manganese ion binding / response to lipopolysaccharide / aging / peptidyl-serine phosphorylation / GTP binding / magnesium ion binding / endoplasmic reticulum / mitochondrion / cytosol / cytoplasm
Similarity search - Function
Phosphoenolpyruvate carboxykinase N-terminal domain / Phosphoenolpyruvate carboxykinase C-terminal P-loop domain / Phosphoenolpyruvate carboxykinase, GTP-utilising / Phosphoenolpyruvate carboxykinase, GTP-utilising, N-terminal / Phosphoenolpyruvate carboxykinase, GTP-utilising, conserved site / Phosphoenolpyruvate carboxykinase (GTP) signature. / Phosphoenolpyruvate carboxykinase, C-terminal P-loop domain / Phosphoenolpyruvate Carboxykinase; domain 3 - #20 / Phosphoenolpyruvate Carboxykinase; domain 2 / Phosphoenolpyruvate Carboxykinase, domain 1 ...Phosphoenolpyruvate carboxykinase N-terminal domain / Phosphoenolpyruvate carboxykinase C-terminal P-loop domain / Phosphoenolpyruvate carboxykinase, GTP-utilising / Phosphoenolpyruvate carboxykinase, GTP-utilising, N-terminal / Phosphoenolpyruvate carboxykinase, GTP-utilising, conserved site / Phosphoenolpyruvate carboxykinase (GTP) signature. / Phosphoenolpyruvate carboxykinase, C-terminal P-loop domain / Phosphoenolpyruvate Carboxykinase; domain 3 - #20 / Phosphoenolpyruvate Carboxykinase; domain 2 / Phosphoenolpyruvate Carboxykinase, domain 1 / Phosphoenolpyruvate Carboxykinase; domain 1 / Phosphoenolpyruvate Carboxykinase, domain 2 / Phosphoenolpyruvate carboxykinase, C-terminal / Phosphoenolpyruvate carboxykinase, N-terminal / Phosphoenolpyruvate Carboxykinase; domain 3 / Beta Complex / Alpha-Beta Complex / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
2-ETHOXYETHANOL / GUANOSINE-5'-TRIPHOSPHATE / SULFOPYRUVATE / : / Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsHolyoak, T.
Funding support Canada, 1items
OrganizationGrant numberCountry
Natural Sciences and Engineering Research Council (NSERC, Canada)Discovery Canada
CitationJournal: Mol.Genet.Metab. / Year: 2014
Title: Three rare diseases in one Sib pair: RAI1, PCK1, GRIN2B mutations associated with Smith-Magenis Syndrome, cytosolic PEPCK deficiency and NMDA receptor glutamate insensitivity.
Authors: Adams, D.R. / Yuan, H. / Holyoak, T. / Arajs, K.H. / Hakimi, P. / Markello, T.C. / Wolfe, L.A. / Vilboux, T. / Burton, B.K. / Fajardo, K.F. / Grahame, G. / Holloman, C. / Sincan, M. / Smith, ...Authors: Adams, D.R. / Yuan, H. / Holyoak, T. / Arajs, K.H. / Hakimi, P. / Markello, T.C. / Wolfe, L.A. / Vilboux, T. / Burton, B.K. / Fajardo, K.F. / Grahame, G. / Holloman, C. / Sincan, M. / Smith, A.C. / Wells, G.A. / Huang, Y. / Vega, H. / Snyder, J.P. / Golas, G.A. / Tifft, C.J. / Boerkoel, C.F. / Hanson, R.W. / Traynelis, S.F. / Kerr, D.S. / Gahl, W.A.
History
DepositionFeb 4, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 11, 2014Provider: repository / Type: Initial release
Revision 1.1Jul 30, 2014Group: Data collection
Revision 1.2Feb 4, 2015Group: Derived calculations
Revision 1.3Feb 11, 2015Group: Database references
Revision 1.4Sep 20, 2017Group: Author supporting evidence / Derived calculations ...Author supporting evidence / Derived calculations / Other / Refinement description / Source and taxonomy
Category: entity_src_gen / pdbx_audit_support ...entity_src_gen / pdbx_audit_support / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_conn_angle / pdbx_struct_oper_list / software
Item: _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization ..._entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_oper_list.symmetry_operation / _software.classification
Revision 1.5Jan 8, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
B: Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)141,30017
Polymers138,9752
Non-polymers2,32515
Water8,233457
1
A: Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,6058
Polymers69,4881
Non-polymers1,1177
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,6959
Polymers69,4881
Non-polymers1,2088
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)61.924, 119.252, 87.397
Angle α, β, γ (deg.)90.000, 106.920, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Phosphoenolpyruvate carboxykinase, cytosolic [GTP] / / PEPCK-C / Phosphoenolpyruvate carboxylase / PEPCK-C / Phosphoenolpyruvate carboxylase


Mass: 69487.609 Da / Num. of mol.: 2 / Mutation: I45T
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Pck1,pck1 / Plasmid: pSumo / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: P07379, phosphoenolpyruvate carboxykinase (GTP)

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Non-polymers , 7 types, 472 molecules

#2: Chemical
ChemComp-MN / MANGANESE (II) ION


Mass: 54.938 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mn
#3: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE / Guanosine triphosphate


Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#4: Chemical ChemComp-SPV / SULFOPYRUVATE


Mass: 168.125 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H4O6S
#5: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#6: Chemical ChemComp-1PE / PENTAETHYLENE GLYCOL / PEG400 / Polyethylene glycol


Mass: 238.278 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H22O6 / Comment: precipitant*YM
#7: Chemical ChemComp-ETX / 2-ETHOXYETHANOL / 2-Ethoxyethanol


Mass: 90.121 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O2
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 457 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.22 Å3/Da / Density % sol: 44.63 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.4 / Details: PEG 3350, HEPES pH 7.4, MnCl2, GTP

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.54 Å
DetectorType: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Apr 19, 2012
RadiationProtocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 2→100 Å / Num. obs: 80162 / % possible obs: 98.4 % / Redundancy: 6.6 % / Rmerge(I) obs: 0.112 / Χ2: 1.055 / Net I/av σ(I): 13.934 / Net I/σ(I): 10.2 / Num. measured all: 525945

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Processing

Software
NameVersionClassification
SCALEPACKdata scaling
HKL-2000data scaling
PDB_EXTRACT3.14data extraction
REFMAC5.7.0029refinement
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3Dt7
Resolution: 2→29.13 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.943 / WRfactor Rfree: 0.2438 / WRfactor Rwork: 0.1994 / FOM work R set: 0.8224 / SU B: 4.524 / SU ML: 0.125 / SU R Cruickshank DPI: 0.2096 / SU Rfree: 0.1753 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.21 / ESU R Free: 0.175 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2328 4021 5 %RANDOM
Rwork0.1889 75998 --
obs0.1911 80019 98.08 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 92.79 Å2 / Biso mean: 34.935 Å2 / Biso min: 18.13 Å2
Baniso -1Baniso -2Baniso -3
1-0.03 Å2-0 Å2-0 Å2
2---0.04 Å2-0 Å2
3---0.01 Å2
Refinement stepCycle: final / Resolution: 2→29.13 Å
LigandSolventTotal
Num. atoms115 457 10254
Biso mean33.32 39.14 -
Num. residues--1228
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.01910048
X-RAY DIFFRACTIONr_bond_other_d0.0010.029646
X-RAY DIFFRACTIONr_angle_refined_deg1.2951.97213620
X-RAY DIFFRACTIONr_angle_other_deg0.7553.00222093
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.31151234
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.38424.186442
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.255151703
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.6721558
X-RAY DIFFRACTIONr_chiral_restr0.0690.21425
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02111286
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022230
LS refinement shellResolution: 2.002→2.054 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.304 264 -
Rwork0.269 5379 -
all-5643 -
obs--94.29 %

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