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- PDB-1gol: COORDINATES OF RAT MAP KINASE ERK2 WITH AN ARGININE MUTATION AT P... -

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Basic information

Entry
Database: PDB / ID: 1gol
TitleCOORDINATES OF RAT MAP KINASE ERK2 WITH AN ARGININE MUTATION AT POSITION 52
ComponentsEXTRACELLULAR REGULATED KINASE 2
KeywordsTRANSFERASE / SERINE/THREONINE-PROTEIN KINASE / ATP-BINDING / CELL CYCLE / PHOSPHORYLATION
Function / homology
Function and homology information


phospho-PLA2 pathway / RAF-independent MAPK1/3 activation / MAPK1 (ERK2) activation / Signaling by NODAL / Frs2-mediated activation / ERK/MAPK targets / ERKs are inactivated / Activation of the AP-1 family of transcription factors / RHO GTPases Activate WASPs and WAVEs / Negative feedback regulation of MAPK pathway ...phospho-PLA2 pathway / RAF-independent MAPK1/3 activation / MAPK1 (ERK2) activation / Signaling by NODAL / Frs2-mediated activation / ERK/MAPK targets / ERKs are inactivated / Activation of the AP-1 family of transcription factors / RHO GTPases Activate WASPs and WAVEs / Negative feedback regulation of MAPK pathway / Gastrin-CREB signalling pathway via PKC and MAPK / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / Golgi Cisternae Pericentriolar Stack Reorganization / Regulation of actin dynamics for phagocytic cup formation / Estrogen-stimulated signaling through PRKCZ / Signaling by Activin / Growth hormone receptor signaling / Spry regulation of FGF signaling / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / Oxidative Stress Induced Senescence / Senescence-Associated Secretory Phenotype (SASP) / Oncogene Induced Senescence / Downregulation of SMAD2/3:SMAD4 transcriptional activity / Signal attenuation / Regulation of the apoptosome activity / NCAM signaling for neurite out-growth / Negative regulation of FGFR1 signaling / Negative regulation of FGFR3 signaling / Negative regulation of FGFR4 signaling / ESR-mediated signaling / Signal transduction by L1 / Negative regulation of FGFR2 signaling / RHO GTPases Activate NADPH Oxidases / Negative regulation of MAPK pathway / FCERI mediated MAPK activation / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / MAP2K and MAPK activation / Regulation of HSF1-mediated heat shock response / diadenosine tetraphosphate biosynthetic process / Recycling pathway of L1 / neural crest cell development / mitogen-activated protein kinase kinase kinase binding / cardiac neural crest cell development involved in heart development / cytosine metabolic process / caveolin-mediated endocytosis / outer ear morphogenesis / response to epidermal growth factor / Thrombin signalling through proteinase activated receptors (PARs) / regulation of cellular pH / regulation of Golgi inheritance / positive regulation of macrophage proliferation / cellular response to granulocyte macrophage colony-stimulating factor stimulus / RAF/MAP kinase cascade / labyrinthine layer blood vessel development / ERBB signaling pathway / trachea formation / Neutrophil degranulation / mammary gland epithelial cell proliferation / lung morphogenesis / regulation of early endosome to late endosome transport / positive regulation of macrophage chemotaxis / regulation of cytoskeleton organization / regulation of stress-activated MAPK cascade / cellular response to organic substance / cellular response to dopamine / response to exogenous dsRNA / face development / pseudopodium / Bergmann glial cell differentiation / thyroid gland development / negative regulation of cell differentiation / positive regulation of telomere capping / decidualization / regulation of ossification / MAP kinase activity / phosphatase binding / mitogen-activated protein kinase / cellular response to amino acid starvation / MAP kinase kinase activity / stress-activated MAPK cascade / positive regulation of cardiac muscle cell proliferation / positive regulation of telomere maintenance via telomerase / dendrite cytoplasm / RNA polymerase II CTD heptapeptide repeat kinase activity / insulin-like growth factor receptor signaling pathway / phosphotyrosine residue binding / positive regulation of telomerase activity / ERK1 and ERK2 cascade / long-term synaptic potentiation / lipopolysaccharide-mediated signaling pathway / sensory perception of pain / cellular response to cadmium ion / response to nicotine / positive regulation of peptidyl-threonine phosphorylation / thymus development / caveola / positive regulation of translation / microtubule organizing center / response to toxic substance / animal organ morphogenesis
Similarity search - Function
Mitogen-activated protein (MAP) kinase, ERK1/2 / Mitogen-activated protein (MAP) kinase, conserved site / MAP kinase signature. / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Protein kinase domain ...Mitogen-activated protein (MAP) kinase, ERK1/2 / Mitogen-activated protein (MAP) kinase, conserved site / MAP kinase signature. / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-TRIPHOSPHATE / Mitogen-activated protein kinase 1
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / Resolution: 2.8 Å
AuthorsHarkins, P.C. / Zhang, F. / Goldsmith, E.J.
Citation
Journal: Biochemistry / Year: 1996
Title: Mutation of position 52 in ERK2 creates a nonproductive binding mode for adenosine 5'-triphosphate.
Authors: Robinson, M.J. / Harkins, P.C. / Zhang, J. / Baer, R. / Haycock, J.W. / Cobb, M.H. / Goldsmith, E.J.
#1: Journal: Structure / Year: 1995
Title: Activity of the Map Kinase Erk2 is Controlled by a Flexible Surface Loop
Authors: Zhang, J. / Zhang, F. / Ebert, D. / Cobb, M.H. / Goldsmith, E.J.
#2: Journal: Nature / Year: 1994
Title: Atomic Structure of the Map Kinase Erk2 at 2.3 A Resolution
Authors: Zhang, F. / Strand, A. / Robbins, D. / Cobb, M.H. / Goldsmith, E.J.
#3: Journal: J.Mol.Biol. / Year: 1993
Title: Crystallization and Preliminary X-Ray Studies of Extracellular Signal-Regulated Kinase-2/Map Kinase with an Incorporated His-Tag
Authors: Zhang, F. / Robbins, D.J. / Cobb, M.H. / Goldsmith, E.J.
History
DepositionJan 23, 1996Processing site: BNL
Revision 1.0Mar 12, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: EXTRACELLULAR REGULATED KINASE 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,7193
Polymers42,1871
Non-polymers5312
Water1,42379
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)49.320, 71.420, 61.250
Angle α, β, γ (deg.)90.00, 109.75, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein EXTRACELLULAR REGULATED KINASE 2 / MAP KINASE ERK2


Mass: 42187.449 Da / Num. of mol.: 1 / Mutation: K52R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Cell line: BL21 / Gene: ERK2 / Plasmid: BL21 / Species (production host): Escherichia coli / Gene (production host): ERK2 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3)
References: UniProt: P63086, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 79 / 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: 2.41 Å3/Da / Density % sol: 48.87 %
Crystal grow
*PLUS
Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
16 mg/mlprotein1drop
218 %PEG80001reservoir
30.2 Mammonium sulfate1reservoir

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Data collection

Diffraction sourceWavelength: 1.5418
DetectorType: RIGAKU / Detector: IMAGE PLATE / Date: Jul 7, 1995 / Details: MIRRORS
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionRedundancy: 4 % / Rmerge(I) obs: 0.056

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Processing

Software
NameClassification
DENZOdata reduction
SCALEPACKdata scaling
RefinementHighest resolution: 2.8 Å
Refinement stepCycle: LAST / Highest resolution: 2.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2901 0 32 79 3012

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