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- PDB-3ro3: crystal structure of LGN/mInscuteable complex -

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Basic information

Entry
Database: PDB / ID: 3ro3
Titlecrystal structure of LGN/mInscuteable complex
Components
  • G-protein-signaling modulator 2
  • peptide of Protein inscuteable homolog
KeywordsPROTEIN BINDING / asymmetric cell division
Function / homology
Function and homology information


lateral cell cortex / cell cortex region / maintenance of centrosome location / regulation of asymmetric cell division / asymmetric cell division / positive regulation of spindle assembly / G alpha (i) signalling events / apical cortex / cytoskeletal anchor activity / apical protein localization ...lateral cell cortex / cell cortex region / maintenance of centrosome location / regulation of asymmetric cell division / asymmetric cell division / positive regulation of spindle assembly / G alpha (i) signalling events / apical cortex / cytoskeletal anchor activity / apical protein localization / GDP-dissociation inhibitor activity / dynein complex binding / mitotic spindle pole / establishment of mitotic spindle orientation / lateral plasma membrane / G-protein alpha-subunit binding / positive regulation of protein localization to cell cortex / regulation of mitotic spindle organization / mitotic spindle organization / regulation of protein stability / nervous system development / cell cortex / cell differentiation / protein domain specific binding / cell division / nucleotide binding / centrosome / protein-containing complex / identical protein binding / plasma membrane / cytosol
Similarity search - Function
Protein inscuteable homologue, LGN-binding domain / Protein inscuteable homologue, LGN-binding domain superfamily / Inscuteable LGN-binding domain / Inscuteable / Protein inscuteable homologue, C-terminal domain / Protein inscuteable C-terminal / : / GoLoco motif / GoLoco motif / GoLoco/GPR motif profile. ...Protein inscuteable homologue, LGN-binding domain / Protein inscuteable homologue, LGN-binding domain superfamily / Inscuteable LGN-binding domain / Inscuteable / Protein inscuteable homologue, C-terminal domain / Protein inscuteable C-terminal / : / GoLoco motif / GoLoco motif / GoLoco/GPR motif profile. / LGN motif, putative GEFs specific for G-alpha GTPases / Tetratricopeptide repeat / Tetratricopeptide repeat / Tetratricopeptide repeat / Tetratricopeptide repeat domain / Armadillo/beta-catenin-like repeats / Armadillo / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Armadillo-like helical / Alpha Horseshoe / Tetratricopeptide-like helical domain superfamily / Armadillo-type fold / Mainly Alpha
Similarity search - Domain/homology
ETHANOL / Protein inscuteable homolog / G-protein-signaling modulator 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.1 Å
AuthorsZhu, J. / Wen, W. / Shang, Y. / Wei, Z. / Pan, Z. / Wang, W. / Zhang, M.
CitationJournal: Mol.Cell / Year: 2011
Title: LGN/mInsc and LGN/NuMA complex structures suggest distinct functions in asymmetric cell division for the Par3/mInsc/LGN and G[alpha]i/LGN/NuMA pathways
Authors: Zhu, J. / Wen, W. / Zheng, Z. / Shang, Y. / Wei, Z. / Xiao, Z. / Pan, Z. / Du, Q. / Wang, W. / Zhang, M.
History
DepositionApr 25, 2011Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Mar 7, 2012Provider: repository / Type: Initial release
Revision 1.1Mar 20, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / 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 / _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

Downloads & links

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Assembly

Deposited unit
A: G-protein-signaling modulator 2
B: peptide of Protein inscuteable homolog
hetero molecules


Theoretical massNumber of molelcules
Total (without water)21,4789
Polymers21,1632
Non-polymers3157
Water5,693316
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1730 Å2
ΔGint-9 kcal/mol
Surface area8910 Å2
MethodPISA
Unit cell
Length a, b, c (Å)88.196, 75.606, 35.346
Angle α, β, γ (deg.)90.00, 105.99, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11A-384-

HOH

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Components

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Protein / Protein/peptide , 2 types, 2 molecules AB

#1: Protein G-protein-signaling modulator 2 / Pins homolog


Mass: 18365.561 Da / Num. of mol.: 1 / Fragment: UNP residues 198-357 / Mutation: R236I
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Gpsm2, Lgn, Pins / Plasmid: pET32a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: Q8VDU0
#2: Protein/peptide peptide of Protein inscuteable homolog / Minsc


Mass: 2797.278 Da / Num. of mol.: 1 / Fragment: UNP residues 66-87 / Source method: obtained synthetically / Details: THE SEQUENCE NATURALLY OCCURS IN MOUSE / Source: (synth.) Mus musculus (house mouse) / References: UniProt: Q3HNM7

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Non-polymers , 4 types, 323 molecules

#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-EOH / ETHANOL


Mass: 46.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O
#5: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 316 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.68 Å3/Da / Density % sol: 54.04 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 1.5M NaCl, 10% Ethanol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 0.9793 Å
DetectorType: RAYONIX MX-225 / Detector: CCD / Date: Dec 9, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 1.1→50 Å / Num. obs: 84934 / Observed criterion σ(I): 2

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Processing

Software
NameClassification
HKL-2000data collection
MLPHAREphasing
SHELXL-97refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.1→20 Å /
RfactorNum. reflection
Rfree0.15 4259
all0.12 -
obs-84907
Refinement stepCycle: LAST / Resolution: 1.1→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1405 0 14 316 1735

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