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- PDB-1ide: ISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE C... -

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Basic information

Entry
Database: PDB / ID: 1ide
TitleISOCITRATE DEHYDROGENASE Y160F MUTANT STEADY-STATE INTERMEDIATE COMPLEX (LAUE DETERMINATION)
ComponentsISOCITRATE DEHYDROGENASE
KeywordsOXIDOREDUCTASE (NAD(A)-CHOH(D))
Function / homology
Function and homology information


isocitrate dehydrogenase (NADP+) / isocitrate dehydrogenase (NADP+) activity / glyoxylate cycle / guanosine tetraphosphate binding / tricarboxylic acid cycle / electron transport chain / NAD binding / response to oxidative stress / magnesium ion binding / cytoplasm / cytosol
Similarity search - Function
Isocitrate dehydrogenase NADP-dependent, dimeric, prokaryotic / Isopropylmalate Dehydrogenase / Isopropylmalate Dehydrogenase / Isocitrate/isopropylmalate dehydrogenase, conserved site / Isocitrate and isopropylmalate dehydrogenases signature. / Isopropylmalate dehydrogenase-like domain / Isocitrate/isopropylmalate dehydrogenase / Isocitrate/isopropylmalate dehydrogenase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ISOCITRIC ACID / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Isocitrate dehydrogenase [NADP]
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.5 Å
AuthorsBolduc, J.M. / Dyer, D.H. / Scott, W.G. / Singer, P. / Sweet, R.M. / Koshland Junior, D.E. / Stoddard, B.L.
Citation
Journal: Science / Year: 1995
Title: Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase.
Authors: Bolduc, J.M. / Dyer, D.H. / Scott, W.G. / Singer, P. / Sweet, R.M. / Koshland Jr., D.E. / Stoddard, B.L.
#1: Journal: Biochemistry / Year: 1991
Title: Catalytic Mechanism of Nadp+-Dependent Isocitrate Dehydrogenase: Implications from the Structures of Magnesium-Isocitrate and Nadp+ Complexes
Authors: Hurley, J.H. / Dean, A.M. / Koshland Junior, D.E. / Stroud, R.M.
#2: Journal: J.Biol.Chem. / Year: 1990
Title: Regulation of Isocitrate Dehydrogenase by Phosphorylation Involves No Long-Range Conformational Change in the Free Enzyme
Authors: Hurley, J.H. / Dean, A.M. / Thorsness, P.E. / Koshland Junior, D.E. / Stroud, R.M.
#3: Journal: Science / Year: 1990
Title: Regulation of an Enzyme by Phosphorylation at the Active Site
Authors: Hurley, J.H. / Dean, A.M. / Sohl, J.L. / Koshland Junior, D.E. / Stroud, R.M.
#4: Journal: Proc.Natl.Acad.Sci.USA / Year: 1989
Title: Structure of a Bacterial Enzyme Regulated by Phosphorylation, Isocitrate Dehydrogenase
Authors: Hurley, J.H. / Thorsness, P.E. / Ramalingam, V. / Helmers, N.H. / Koshland Junior, D.E. / Stroud, R.M.
History
DepositionJan 18, 1995Processing site: BNL
Revision 1.0Mar 8, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Nov 3, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_conn_angle ...database_2 / 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_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.ptnr1_symmetry / _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.ptnr3_symmetry / _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.ptnr1_symmetry / _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_conn.ptnr2_symmetry / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Feb 7, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ISOCITRATE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,7534
Polymers45,7941
Non-polymers9603
Water362
1
A: ISOCITRATE DEHYDROGENASE
hetero molecules

A: ISOCITRATE DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,5078
Polymers91,5872
Non-polymers1,9206
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_555y,x,-z1
Buried area10070 Å2
ΔGint-58 kcal/mol
Surface area31370 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)105.100, 105.100, 150.300
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212
Atom site foot note1: CIS PROLINE - PRO 262

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Components

#1: Protein ISOCITRATE DEHYDROGENASE / IDH


Mass: 45793.562 Da / Num. of mol.: 1 / Mutation: Y160F
Source method: isolated from a genetically manipulated source
Details: TERNARY RATE-LIMITED MICHAELIS COMPLEX / Source: (gene. exp.) Escherichia coli (E. coli) / Strain: JLK1 / Gene: ICD / Variant: ICD(-) (DEFICIENT IN WT IDH GENE) / Plasmid: PTK513 / Gene (production host): ICD
Production host: PEMBL (DENTE ET AL 1983 NUC ACIDS RES 11,1645)
References: UniProt: P08200, isocitrate dehydrogenase (NADP+)
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-ICT / ISOCITRIC ACID


Mass: 192.124 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H8O7
#4: Chemical ChemComp-NAP / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE


Mass: 743.405 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C21H28N7O17P3
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: H2O
Compound detailsTHE NICOTINAMIDE RING IN THIS Y160F DYNAMIC LAUE STRUCTURE SHOWS VERY CLEAR SIGNS OF OCCUPYING AT ...THE NICOTINAMIDE RING IN THIS Y160F DYNAMIC LAUE STRUCTURE SHOWS VERY CLEAR SIGNS OF OCCUPYING AT LEAST TWO DISTINCT CONFORMERS. THIS IS DUE TO THE FACT THAT THE ENZYME IS TURNING OVER IN THE PRESENCE OF SATURATING SUBSTRATE CONCENTRATIONS WHEN THE DATA IS COLLECTED IN THIS EXPERIMENT, AND THE NICOTINAMIDE RING IS THE MOST MOBILE STRUCTURAL ELEMENT IN THE FULL ENZYMATIC COMPLEX. THE ELECTRON DENSITY FIGURE IN THE SCIENCE MANUSCRIPT FOR Y160F INDICATES A LARGE DEGREE OF FREEDOM FOR THE NICOTINAMIDE RING. THE STRUCTURE AND ORIENTATION OF THE RING IN THIS COORDINATE SET SHOWS A SLIGHT ROTATION ABOUT THE GLYCOSIDIC RIBOSYL-NICOTINAMIDE BOND RELATIVE TO THE FIGURE IN THE PAPER; BOTH CONFORMERS HAVE BEEN INDEPENDENTLY REFINED BUT THE AUTHORS HAVE DECIDED TO FAVOR THIS MODEL IN THE FINAL DEPOSITED STRUCTURE AS IT (1) AGREES WELL WITH MOLECULAR DYNAMICS SIMULATIONS, (2) HAS GOOD GEOMETRY AND CONTACTS, (3) HAS AN ORIENTATION OF THE NADP THAT AGREES WELL WITH OTHER DEHYDROGENASE COMPLEX STRUCTURES, AND (4) AGREES WITH THE STRUCTURE OF THE BINARY ISOCITRATE/MG+2 STRUCTURE (HURLEY ET AL. SCIENCE 1990, 249: 1012) AND THE STRUCTURE OF THE INACTIVE CALCIUM-COMPLEX (STODDARD ET AL. BIOCHEMISTRY 1993 32: 9310.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 4.53 Å3/Da / Density % sol: 72.85 %
Crystal
*PLUS
Density % sol: 73 %
Crystal grow
*PLUS
pH: 5.4 / Method: unknown
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
128 mg/mldephosphorylated IDH1reservoir
234 %satammonium sulfate1reservoir
3100 mM1reservoirNaCl
435 mM1reservoirNa2HPO4
59 mMcitric acid1reservoir
60.2 mMdithiothreitol1reservoir

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 0.7 - 2.1
DetectorType: FUJI / Detector: IMAGE PLATE / Date: Oct 15, 1993
RadiationProtocol: LAUE / Monochromatic (M) / Laue (L): L / Scattering type: neutron
Radiation wavelength
IDWavelength (Å)Relative weight
10.71
22.11
ReflectionNum. obs: 17043 / % possible obs: 61 % / Observed criterion σ(I): 1 / Redundancy: 17.3 % / Rmerge(I) obs: 0.084
Reflection
*PLUS
Highest resolution: 2.5 Å / Lowest resolution: 100 Å / Rmerge(I) obs: 0.084

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
OXFORDLAUE PACKAGE (J.CAMPBELL)data reduction
X-PLOR3.1phasing
RefinementHighest resolution: 2.5 Å / σ(F): 2
Details: DATA COLLECTED FROM FOUR SEPARATE CRYSTALS AT X26-C (POLYCHROMATIC LAUE BEAM LINE AT BROOKHAVEN NATIONAL LABORATORY) AND MERGED TOGETHER WITH LAUENORM IN OXFORD LAUE DATA REDUCTION PACKAGE
RfactorNum. reflection
Rwork0.192 -
obs0.192 17043
Refinement stepCycle: LAST / Highest resolution: 2.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3195 0 62 2 3259
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.019
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg3.794
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d26.2
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d2.539
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Software
*PLUS
Name: X-PLOR / Classification: refinement
Refinement
*PLUS
Lowest resolution: 10 Å
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg26.2
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg2.539

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