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- PDB-1c0f: CRYSTAL STRUCTURE OF DICTYOSTELIUM CAATP-ACTIN IN COMPLEX WITH GE... -

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Basic information

Entry
Database: PDB / ID: 1c0f
TitleCRYSTAL STRUCTURE OF DICTYOSTELIUM CAATP-ACTIN IN COMPLEX WITH GELSOLIN SEGMENT 1
Components
  • ACTIN
  • GELSOLIN SEGMENT 1
KeywordsCONTRACTILE PROTEIN / CA ACTIN
Function / homology
Function and homology information


intranuclear rod / phototaxis / phagolysosome / cell pole / positive regulation of keratinocyte apoptotic process / striated muscle atrophy / renal protein absorption / regulation of establishment of T cell polarity / regulation of plasma membrane raft polarization / regulation of receptor clustering ...intranuclear rod / phototaxis / phagolysosome / cell pole / positive regulation of keratinocyte apoptotic process / striated muscle atrophy / renal protein absorption / regulation of establishment of T cell polarity / regulation of plasma membrane raft polarization / regulation of receptor clustering / positive regulation of protein processing in phagocytic vesicle / positive regulation of actin nucleation / actin cap / sequestering of actin monomers / regulation of podosome assembly / positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway / myosin II binding / sarcoplasm / negative regulation of viral entry into host cell / actin filament severing / actin nucleation / barbed-end actin filament capping / hyperosmotic response / early phagosome / actin filament capping / tissue regeneration / oligodendrocyte development / phagocytic cup / myosin binding / response to folic acid / cortical actin cytoskeleton / podosome / cell leading edge / pseudopodium / lipid droplet / hepatocyte apoptotic process / cilium assembly / phagocytosis / mitotic cytokinesis / regulation of cell adhesion / phagocytic vesicle / actin filament polymerization / response to cAMP / actin filament reorganization / endocytic vesicle / vesicle-mediated transport / actin filament / structural constituent of cytoskeleton / cellular response to interferon-gamma / phosphatidylinositol-mediated signaling / ruffle / phagocytosis, engulfment / protein destabilization / cellular response to cadmium ion / cell morphogenesis / cell cortex / actin cytoskeleton / endocytosis / actin filament binding / chemotaxis / lamellipodium / myelin sheath / actin binding / amyloid fibril formation / secretory granule lumen / ficolin-1-rich granule lumen / response to ethanol / blood microparticle / aging / focal adhesion / cellular protein metabolic process / positive regulation of gene expression / neutrophil degranulation / calcium ion binding / perinuclear region of cytoplasm / protein-containing complex / cell / extracellular space / extracellular exosome / extracellular region / ATP binding / plasma membrane / cytosol / cytoplasm
Gelsolin repeat / Actin / Gelsolin / ADF-H/Gelsolin-like domain superfamily / Actin/actin-like conserved site / Gelsolin-like domain / Villin/Gelsolin / Actin, conserved site / Actin family / Severin ...Gelsolin repeat / Actin / Gelsolin / ADF-H/Gelsolin-like domain superfamily / Actin/actin-like conserved site / Gelsolin-like domain / 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
Major actin / Gelsolin
Biological speciesHomo sapiens (human)
Dictyostelium discoideum (eukaryote)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.4 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
S: GELSOLIN SEGMENT 1
A: ACTIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)55,7906
Polymers55,1632
Non-polymers6274
Water7,224401
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3640 Å2
ΔGint-53 kcal/mol
Surface area21140 Å2
MethodPISA
Unit cell
γ
α
β
Length a, b, c (Å)57.000, 69.550, 184.620
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 GELSOLIN SEGMENT 1


Mass: 14205.001 Da / Num. of mol.: 1 / Mutation: N35C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P06396
#2: Protein ACTIN /


Mass: 40957.543 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) 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.: 401 / 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: 3.32 Å3/Da / Density % sol: 62.9 %
Crystal growTemperature: 290 K / Method: vapor diffusion, hanging drop / pH: 6.6
Details: IMIDAZOLE, SODIUM CHLORIDE, ATP, CALCIUM CHLORIDE, MAGNESIUM CHLORIDE, SODIUM AZIDE, DITHIOTHREITOL, PEG 6000, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 290K
Crystal grow
*PLUS
pH: 7
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: SRS / Beamline: PX9.6 / Wavelength: 0.87
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 5, 1998
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.87 Å / Relative weight: 1
ReflectionResolution: 2.4→29.1 Å / Num. obs: 27962 / % possible obs: 94.4 % / Rmerge(I) obs: 0.074 / Net I/σ(I): 8
Reflection shellResolution: 2.4→2.52 Å / Rmerge(I) obs: 0.155
Reflection
*PLUS
% possible obs: 94.9 % / Num. measured all: 68469
Reflection shell
*PLUS
Mean I/σ(I) obs: 4.5

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
SCALAdata scaling
REFMACrefinement
CCP4(SCALA)data scaling
RefinementResolution: 2.4→10 Å / Cross valid method: THROUGHOUT /
RfactorSelection details
Rfree0.231 RANDOM
Rwork0.183 -
Refinement stepCycle: LAST / Resolution: 2.4→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3877 0 34 401 4312
Refine LS restraints
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONp_bond_d
X-RAY DIFFRACTIONp_angle_d1.9
X-RAY DIFFRACTIONp_angle_deg1.9
X-RAY DIFFRACTIONp_planar_d
X-RAY DIFFRACTIONp_hb_or_metal_coord
X-RAY DIFFRACTIONp_mcbond_it
X-RAY DIFFRACTIONp_mcangle_it
X-RAY DIFFRACTIONp_scbond_it
X-RAY DIFFRACTIONp_scangle_it
X-RAY DIFFRACTIONp_plane_restr
X-RAY DIFFRACTIONp_chiral_restr
X-RAY DIFFRACTIONp_singtor_nbd
X-RAY DIFFRACTIONp_multtor_nbd
X-RAY DIFFRACTIONp_xhyhbond_nbd
X-RAY DIFFRACTIONp_xyhbond_nbd
X-RAY DIFFRACTIONp_planar_tor
X-RAY DIFFRACTIONp_staggered_tor
X-RAY DIFFRACTIONp_orthonormal_tor
X-RAY DIFFRACTIONp_transverse_tor
X-RAY DIFFRACTIONp_special_tor
Software
*PLUS
Name: REFMAC / Classification: refinement
Refine LS restraints
*PLUS
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONp_bond_d0.01
X-RAY DIFFRACTIONp_angle_d

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