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- PDB-1djw: PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEX... -

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Basic information

Entry
Database: PDB / ID: 1djw
TitlePHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C-DELTA1 FROM RAT COMPLEXED WITH INOSITOL-2-METHYLENE-1,2-CYCLIC-MONOPHOSPHONATE
ComponentsPHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
KeywordsLIPID DEGRADATION / PHOSPHORIC DIESTER HYDROLASE / HYDROLASE / TRANSDUCER / CALCIUM-BINDING / PHOSPHOLIPASE C / PHOSPHOINOSITIDE-SPECIFIC
Function / homology
Function and homology information


regulation of phospholipase C activity / response to prostaglandin F / positive regulation of inositol trisphosphate biosynthetic process / Synthesis of IP3 and IP4 in the cytosol / phosphoinositide phospholipase C / positive regulation of norepinephrine secretion / phosphatidylinositol metabolic process / positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway / inositol 1,4,5 trisphosphate binding / response to aluminum ion ...regulation of phospholipase C activity / response to prostaglandin F / positive regulation of inositol trisphosphate biosynthetic process / Synthesis of IP3 and IP4 in the cytosol / phosphoinositide phospholipase C / positive regulation of norepinephrine secretion / phosphatidylinositol metabolic process / positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway / inositol 1,4,5 trisphosphate binding / response to aluminum ion / phosphatidylinositol phospholipase C activity / calcium-dependent phospholipid binding / labyrinthine layer blood vessel development / GTPase activating protein binding / response to hyperoxia / phosphatidylinositol-mediated signaling / lipid catabolic process / response to organonitrogen compound / regulation of cytosolic calcium ion concentration / mitochondrial membrane / response to peptide hormone / phosphatidylinositol-4,5-bisphosphate binding / phospholipid binding / response to calcium ion / regulation of cell population proliferation / angiogenesis / G protein-coupled receptor signaling pathway / membrane raft / calcium ion binding / membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 / Pleckstrin homology domain / Phosphoinositide-specific phospholipase C, efhand-like / Phosphoinositide-specific phospholipase C, EF-hand-like domain / Phosphatidylinositol-specific phospholipase Y-box domain profile. / Phosphatidylinositol-specific phospholipase C, Y domain / Phospholipase C, phosphatidylinositol-specific, Y domain / Phosphoinositide phospholipase C family / Phospholipase C, catalytic domain (part); domain Y / Phosphatidylinositol (PI) phosphodiesterase ...1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1 / Pleckstrin homology domain / Phosphoinositide-specific phospholipase C, efhand-like / Phosphoinositide-specific phospholipase C, EF-hand-like domain / Phosphatidylinositol-specific phospholipase Y-box domain profile. / Phosphatidylinositol-specific phospholipase C, Y domain / Phospholipase C, phosphatidylinositol-specific, Y domain / Phosphoinositide phospholipase C family / Phospholipase C, catalytic domain (part); domain Y / Phosphatidylinositol (PI) phosphodiesterase / Phosphatidylinositol-specific phospholipase X-box domain profile. / Phosphatidylinositol-specific phospholipase C, X domain / Phosphatidylinositol-specific phospholipase C, X domain / Phospholipase C, catalytic domain (part); domain X / PLC-like phosphodiesterase, TIM beta/alpha-barrel domain superfamily / C2 domain / C2 domain / Protein kinase C conserved region 2 (CalB) / C2 domain / C2 domain profile. / EF-hand / C2 domain superfamily / Recoverin; domain 1 / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / EF-hand domain pair / PH-like domain superfamily / TIM Barrel / Alpha-Beta Barrel / Immunoglobulin-like / Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / INOSITOL-2-METHYLENE-1,2-CYCLIC-MONOPHOSPHATE / 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.45 Å
AuthorsEssen, L.-O. / Perisic, O. / Williams, R.L.
Citation
Journal: Biochemistry / Year: 1997
Title: Structural mapping of the catalytic mechanism for a mammalian phosphoinositide-specific phospholipase C.
Authors: Essen, L.O. / Perisic, O. / Katan, M. / Wu, Y. / Roberts, M.F. / Williams, R.L.
#1: Journal: Nature / Year: 1996
Title: Crystal Structure of a Mammalian Phosphoinositide-Specific Phospholipase C Delta
Authors: Essen, L.O. / Perisic, O. / Cheung, R. / Katan, M. / Williams, R.L.
History
DepositionAug 24, 1996-
Revision 1.0Jul 23, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
B: PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)141,98812
Polymers141,1492
Non-polymers83910
Water13,547752
1
A: PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,9946
Polymers70,5751
Non-polymers4195
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,9946
Polymers70,5751
Non-polymers4195
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
γ
α
β
Length a, b, c (Å)397.030, 397.030, 397.030
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number210
Space group name H-MF4132

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Components

#1: Protein PHOSPHOINOSITIDE-SPECIFIC PHOSPHOLIPASE C, ISOZYME DELTA1 / PLC-D1


Mass: 70574.516 Da / Num. of mol.: 2 / Mutation: DELTA(1-132) DELETION VARIANT
Source method: isolated from a genetically manipulated source
Details: CATALYTICALLY-ACTIVE DELETION VARIANT THAT LACKS AN N-TERMINAL PH DOMAIN, COMPLEXED WITH INOSITOL-2-METHYLENE-1,2-CYCLIC-MONOPHOSPHONATE
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: CDNA FRAGMENT / Plasmid: PGEX (PHARMACIA) / Gene (production host): CDNA FRAGMENT / Production host: Escherichia coli (E. coli)
References: UniProt: P10688, phosphoinositide phospholipase C
#2: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Ca
#3: Chemical ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#4: Chemical ChemComp-CIP / INOSITOL-2-METHYLENE-1,2-CYCLIC-MONOPHOSPHATE


Mass: 240.148 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C7H13O7P
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 752 / 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: 4.62 Å3/Da / Density % sol: 70 %
Description: DATA COLLECTED AT 100 K FROM SINGLE FROZEN CRYSTAL
Crystal grow
*PLUS
Temperature: 12 ℃ / Method: vapor diffusion, hanging drop / Details: macroseeding
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
110 mg/mlprotein1drop
20.1 %(w/v)CHAPSO1drop
32.0 Mammonium phosphate1drop
41 mMdithiothreitol1drop
51.45 Mammonium phosphate1reservoir
61 mMdithiothreitol1reservoir

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID2 / Wavelength: 0.89
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 4, 1995
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.89 Å / Relative weight: 1
ReflectionNum. obs: 95932 / % possible obs: 98.5 % / Observed criterion σ(I): -3 / Redundancy: 5.2 % / Rmerge(I) obs: 0.067
Reflection
*PLUS
Highest resolution: 2.45 Å / Lowest resolution: 52 Å / Num. measured all: 495077
Reflection shell
*PLUS
% possible obs: 97.4 % / Redundancy: 4.4 % / Rmerge(I) obs: 0.316 / Mean I/σ(I) obs: 4.4

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Processing

Software
NameVersionClassification
TNT5Erefinement
MOSFLMdata reduction
RefinementResolution: 2.45→10 Å / Cross valid method: FREE R-FACTOR / σ(F): 0
Details: THE OCCUPANCY OF INOSITOL-2-METHYLENE-1,2-CYCLIC-MONOPHOSPHONATE WAS REFINED TO 0.65.
RfactorNum. reflection% reflectionSelection details
Rfree0.27 4417 4 %RANDOM SHELLS
Rwork0.217 ---
all-90227 --
obs-90227 96 %-
Refinement stepCycle: LAST / Resolution: 2.45→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8522 0 44 752 9318
Refine LS restraints
Refine-IDTypeDev idealNumberWeight
X-RAY DIFFRACTIONt_bond_d0.01387571
X-RAY DIFFRACTIONt_angle_deg
X-RAY DIFFRACTIONt_dihedral_angle_d
X-RAY DIFFRACTIONt_incorr_chiral_ct0
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes
X-RAY DIFFRACTIONt_gen_planes
X-RAY DIFFRACTIONt_it2.3187855
X-RAY DIFFRACTIONt_nbd
Software
*PLUS
Name: TNT / Version: 5E / Classification: refinement
Refinement
*PLUS
Num. reflection obs: 94320 / Rfactor obs: 0.215
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 44 Å2
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONt_bond_d0.012
X-RAY DIFFRACTIONt_angle_d
X-RAY DIFFRACTIONt_angle_deg1.287
X-RAY DIFFRACTIONt_dihedral_angle_deg18.6
X-RAY DIFFRACTIONt_plane_restr0.013

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