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- PDB-1ef1: CRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX -

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Basic information

Entry
Database: PDB / ID: 1ef1
TitleCRYSTAL STRUCTURE OF THE MOESIN FERM DOMAIN/TAIL DOMAIN COMPLEX
Components(MOESIN) x 2
KeywordsMEMBRANE PROTEIN / membrane / FERM domain / Tail domain
Function / homology
Function and homology information


regulation of lymphocyte migration / T cell aggregation / regulation of organelle assembly / T cell migration / positive regulation of early endosome to late endosome transport / membrane to membrane docking / uropod / immunological synapse formation / gland morphogenesis / positive regulation of protein localization to early endosome ...regulation of lymphocyte migration / T cell aggregation / regulation of organelle assembly / T cell migration / positive regulation of early endosome to late endosome transport / membrane to membrane docking / uropod / immunological synapse formation / gland morphogenesis / positive regulation of protein localization to early endosome / cellular response to testosterone stimulus / establishment of epithelial cell apical/basal polarity / establishment of endothelial barrier / positive regulation of podosome assembly / Sensory processing of sound by outer hair cells of the cochlea / Sensory processing of sound by inner hair cells of the cochlea / microvillus membrane / regulation of cell size / leukocyte cell-cell adhesion / leukocyte migration / Recycling pathway of L1 / pseudopodium / microvillus / Signaling by ALK fusions and activated point mutants / T cell proliferation / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / cell adhesion molecule binding / filopodium / cell periphery / adherens junction / structural constituent of cytoskeleton / positive regulation of protein catabolic process / double-stranded RNA binding / apical part of cell / actin binding / regulation of cell shape / basolateral plasma membrane / blood microparticle / vesicle / cytoskeleton / apical plasma membrane / signaling receptor binding / focal adhesion / positive regulation of gene expression / protein kinase binding / perinuclear region of cytoplasm / enzyme binding / cell surface / extracellular space / extracellular exosome / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #10 / Ezrin/radixin/moesin, alpha-helical domain / Ezrin/radixin/moesin, alpha-helical domain / Moesin tail domain superfamily / Ezrin/radixin/moesin / Ezrin/radixin/moesin, C-terminal / ERM family, FERM domain C-lobe / Ezrin/radixin/moesin family C terminal / Acyl-CoA Binding Protein - #10 ...Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #10 / Ezrin/radixin/moesin, alpha-helical domain / Ezrin/radixin/moesin, alpha-helical domain / Moesin tail domain superfamily / Ezrin/radixin/moesin / Ezrin/radixin/moesin, C-terminal / ERM family, FERM domain C-lobe / Ezrin/radixin/moesin family C terminal / Acyl-CoA Binding Protein - #10 / Ezrin/radixin/moesin-like / Acyl-CoA Binding Protein / FERM, C-terminal PH-like domain / FERM C-terminal PH-like domain / FERM C-terminal PH-like domain / FERM, N-terminal / FERM N-terminal domain / FERM domain signature 1. / FERM conserved site / FERM domain signature 2. / FERM central domain / FERM/acyl-CoA-binding protein superfamily / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / FERM central domain / PH-domain like / FERM superfamily, second domain / FERM domain / FERM domain profile. / Band 4.1 domain / Band 4.1 homologues / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Helix non-globular / Special / Ubiquitin-like (UB roll) / PH-like domain superfamily / Ubiquitin-like domain superfamily / Roll / Roll / Up-down Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.9 Å
AuthorsPearson, M.A. / Reczek, D. / Bretscher, A. / Karplus, P.A.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2000
Title: Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain.
Authors: Pearson, M.A. / Reczek, D. / Bretscher, A. / Karplus, P.A.
History
DepositionFeb 4, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 10, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MOESIN
C: MOESIN
B: MOESIN
D: MOESIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)91,0236
Polymers90,8314
Non-polymers1922
Water7,422412
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: MOESIN
D: MOESIN
hetero molecules

B: MOESIN
D: MOESIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)91,0236
Polymers90,8314
Non-polymers1922
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_566x,-y+1,-z+11
Buried area13880 Å2
ΔGint-96 kcal/mol
Surface area35120 Å2
MethodPISA, PQS
3
A: MOESIN
C: MOESIN
hetero molecules

A: MOESIN
C: MOESIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)91,0236
Polymers90,8314
Non-polymers1922
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_576x,-y+2,-z+11
MethodPQS
Unit cell
Length a, b, c (Å)54.200, 153.300, 112.100
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number17
Space group name H-MP2221
Components on special symmetry positions
IDModelComponents
11A-2001-

SO4

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Components

#1: Protein MOESIN /


Mass: 34846.328 Da / Num. of mol.: 2 / Fragment: N-TERMINAL FERM DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P26038
#2: Protein MOESIN /


Mass: 10569.288 Da / Num. of mol.: 2 / Fragment: C-TERMINAL TAIL DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: P26038
#3: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 412 / 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: 2

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Sample preparation

CrystalDensity Matthews: 2.56 Å3/Da / Density % sol: 52.01 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.8
Details: PEG3350, lithium sulfate, HEPES, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Crystal grow
*PLUS
Temperature: 4 ℃ / pH: 7.5
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
15 mg/mlprotein1drop
210 mMHEPES1drop
320 mM1dropNaCl
41 mMEDTA1drop
55 mMdithiothreitol1drop
6100 mMHEPES1reservoir
7100-150 mM1reservoirLi2SO4
818-20 %PEG33501reservoir

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
Diffraction source
SourceSiteBeamlineIDWavelength
SYNCHROTRONCHESS F110.918
SYNCHROTRONCHESS F22
Detector
TypeIDDetectorDate
ADSC QUANTUM 41CCDMar 15, 1998
ADSC Q42CCDMay 15, 1998
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.918 Å / Relative weight: 1
ReflectionResolution: 1.9→100 Å / Num. obs: 71584 / % possible obs: 95 % / Redundancy: 3.6 %
Reflection shellHighest resolution: 1.9 Å / Redundancy: 3.7 % / % possible all: 92
Reflection
*PLUS
Rmerge(I) obs: 0.09
Reflection shell
*PLUS
Rmerge(I) obs: 0.445

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Processing

Software
NameVersionClassification
MADSYSphasing
X-PLOR3.851refinement
MOSFLMdata reduction
CCP4(SCALA)data scaling
RefinementResolution: 1.9→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.287 3568 random
Rwork0.227 --
obs-66990 -
Refinement stepCycle: LAST / Resolution: 1.9→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6266 0 10 412 6688
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.016
X-RAY DIFFRACTIONx_angle_deg1.7
Software
*PLUS
Name: X-PLOR / Version: 3.851 / Classification: refinement
Refinement
*PLUS
Highest resolution: 1.9 Å / Lowest resolution: 20 Å / σ(F): 0 / Rfactor obs: 0.227
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Type: x_angle_deg / Dev ideal: 1.7

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