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- PDB-1c0g: CRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A... -

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Basic information

Entry
Database: PDB / ID: 1c0g
TitleCRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 228: Q228K/T229A/A230Y/E360H)
Components
  • PROTEIN (CHIMERIC ACTIN)
  • PROTEIN (GELSOLIN SEGMENT 1)
KeywordsCONTRACTILE PROTEIN / ACTIN MUTANT
Function / homology
Function and homology information


intranuclear rod / leading edge of lamellipodium / phototaxis / macropinocytic cup / phagolysosome / cell pole / striated muscle atrophy / renal protein absorption / regulation of establishment of T cell polarity / positive regulation of keratinocyte apoptotic process ...intranuclear rod / leading edge of lamellipodium / phototaxis / macropinocytic cup / phagolysosome / cell pole / striated muscle atrophy / renal protein absorption / regulation of establishment of T cell polarity / positive regulation of keratinocyte apoptotic process / regulation of plasma membrane raft polarization / regulation of receptor clustering / positive regulation of protein processing in phagocytic vesicle / actin cap / positive regulation of actin nucleation / sequestering of actin monomers / regulation of podosome assembly / positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / myosin II binding / sarcoplasm / cell-cell contact zone / negative regulation of viral entry into host cell / actin filament severing / actin nucleation / barbed-end actin filament capping / hyperosmotic response / early phagosome / actin polymerization or depolymerization / actin filament capping / cell projection assembly / tissue regeneration / myosin binding / oligodendrocyte development / response to folic acid / cortical actin cytoskeleton / phagocytic cup / podosome / hepatocyte apoptotic process / pseudopodium / phagocytosis / cilium assembly / cell leading edge / lipid droplet / regulation of cell adhesion / mitotic cytokinesis / phagocytic vesicle / actin filament polymerization / response to cAMP / central nervous system development / endocytic vesicle / phosphatidylinositol-mediated signaling / vesicle-mediated transport / actin filament / ruffle / cellular response to interferon-gamma / actin filament reorganization / phagocytosis, engulfment / structural constituent of cytoskeleton / phosphatidylinositol-4,5-bisphosphate binding / protein destabilization / cell morphogenesis / cellular response to cadmium ion / cell cortex / endocytosis / actin cytoskeleton / actin filament binding / chemotaxis / lamellipodium / actin binding / myelin sheath / amyloid fibril formation / secretory granule lumen / response to ethanol / blood microparticle / ficolin-1-rich granule lumen / aging / focal adhesion / cellular protein metabolic process / positive regulation of gene expression / neutrophil degranulation / calcium ion binding / perinuclear region of cytoplasm / protein-containing complex / extracellular space / extracellular exosome / extracellular region / ATP binding / plasma membrane / cytosol / cytoplasm
Gelsolin-like domain / Gelsolin repeat / Actin / ATPase, nucleotide binding domain / Gelsolin / ADF-H/Gelsolin-like domain superfamily / Actin/actin-like conserved site / Villin/Gelsolin / Actin, conserved site / Actin family ...Gelsolin-like domain / Gelsolin repeat / Actin / ATPase, nucleotide binding domain / Gelsolin / ADF-H/Gelsolin-like domain superfamily / Actin/actin-like conserved site / Villin/Gelsolin / Actin, conserved site / Actin family / Severin / Severin / ATPase, substrate binding domain, subdomain 4 / Actin; Chain A, domain 4 / ATPase, nucleotide binding domain / Nucleotidyltransferase; domain 5 / Alpha-Beta Complex / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Gelsolin / Major actin
Biological speciesHomo sapiens (human)
Dictyostelium discoideum (eukaryote)
Tetrahymena thermophila (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2 Å
AuthorsMatsuura, Y. / Stewart, M. / Kawamoto, M. / Kamiya, N. / Saeki, K. / Yasunaga, T. / Wakabayashi, T.
Citation
Journal: J.Mol.Biol. / Year: 2000
Title: Structural basis for the higher Ca(2+)-activation of the regulated actin-activated myosin ATPase observed with Dictyostelium/Tetrahymena actin chimeras.
Authors: Matsuura, Y. / Stewart, M. / Kawamoto, M. / Kamiya, N. / Saeki, K. / Yasunaga, T. / Wakabayashi, T.
#1: Journal: Nature / Year: 1993
Title: Structure of Gelsolin Segment 1-Actin Complex and the Mechanism of Filament Severing
Authors: Mclaughlin, P.J. / Gooch, J.T. / Mannherz, H.G. / Weeds, A.G.
Validation Report
SummaryFull reportAbout validation report
History
DepositionJul 16, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 1, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 4, 2017Group: Advisory / Refinement description
Category: pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / software

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
S: PROTEIN (GELSOLIN SEGMENT 1)
A: PROTEIN (CHIMERIC ACTIN)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,5656
Polymers55,9382
Non-polymers6274
Water8,449469
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3660 Å2
ΔGint-53 kcal/mol
Surface area21090 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)56.862, 69.030, 181.500
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein PROTEIN (GELSOLIN SEGMENT 1)


Mass: 14205.001 Da / Num. of mol.: 1 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Bacteria (eubacteria) / References: UniProt: P06396
#2: Protein PROTEIN (CHIMERIC ACTIN)


Mass: 41732.578 Da / Num. of mol.: 1 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Dictyostelium discoideum, Tetrahymena thermophila
Genus: Dictyostelium, Tetrahymena / Species: , / Strain: , / Production host: Dictyostelium discoideum (eukaryote) / References: UniProt: P07830
#3: Chemical ChemComp-CA / CALCIUM ION / Calcium


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca
#4: 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
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 469 / 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: 3.18 Å3/Da / Density % sol: 61.35 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6
Details: MES, SODIUM CHLORIDE, ATP, CALCIUM CHLORIDE, MAGNESIUM CHLORIDE, SODIUM AZIDE, DITHIOTHREITOL, PEG 6000, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
Crystal grow
*PLUS
pH: 7 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
15 mg/mlprotein1drop
210 mMimidazole-HCl1drop
3150 mM1dropNaCl
40.1 mMATP1drop
50.1 mM1dropCaCl2
60.1 mM1dropMgCl2
71 mM1dropNaN3
80.1 mMdithiothreitol1drop
950 mMimidazole-HCl1reservoir
10150 mM1reservoirNaCl
110.1 mMATP1reservoir
120.1 mM1reservoirCaCl2
130.1 mM1reservoirMgCl2
141 mM1reservoirNaN3
1510 mMdithiothreitol1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 0.708 / Wavelength: 0.708 Å
DetectorType: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 23, 1998
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.708 Å / Relative weight: 1
ReflectionResolution: 2→30 Å / Num. obs: 45284 / % possible obs: 92.6 % / Rmerge(I) obs: 0.064 / Net I/σ(I): 8
Reflection shellResolution: 2→2.11 Å / Rmerge(I) obs: 0.149
Reflection
*PLUS
Highest resolution: 2 Å / Lowest resolution: 30 Å / Num. measured all: 161420 / Rmerge(I) obs: 0.064
Reflection shell
*PLUS
Highest resolution: 2 Å / Rmerge(I) obs: 0.149 / Mean I/σ(I) obs: 4.6

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Processing

Software
NameVersionClassification
REFMACrefinement
CCP4(SCALA)data scaling
RefinementResolution: 2→10 Å /
RfactorSelection details
Rfree0.223 RANDOM
Rwork0.182 -
Refinement stepCycle: LAST / Resolution: 2→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3883 0 34 469 4386
Refinement
*PLUS
Highest resolution: 2 Å / % reflection Rfree: 5 % / Rfactor Rfree: 0.223 / Rfactor Rwork: 0.182
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONbond_d0.011
X-RAY DIFFRACTIONangle_d
X-RAY DIFFRACTIONangle_deg1.9

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