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- PDB-1s2h: The Mad2 spindle checkpoint protein possesses two distinct native... -

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Basic information

Entry
Database: PDB / ID: 1s2h
TitleThe Mad2 spindle checkpoint protein possesses two distinct natively folded states
ComponentsMitotic spindle assembly checkpoint protein MAD2A
KeywordsCELL CYCLE / Mad2 / spindle checkpoint protein
Function / homology
Function and homology information


mitotic spindle assembly checkpoint MAD1-MAD2 complex / Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components / mitotic checkpoint complex / positive regulation of mitotic cell cycle spindle assembly checkpoint / establishment of centrosome localization / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / nuclear pore nuclear basket / negative regulation of mitotic cell cycle / negative regulation of ubiquitin protein ligase activity ...mitotic spindle assembly checkpoint MAD1-MAD2 complex / Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components / mitotic checkpoint complex / positive regulation of mitotic cell cycle spindle assembly checkpoint / establishment of centrosome localization / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / nuclear pore nuclear basket / negative regulation of mitotic cell cycle / negative regulation of ubiquitin protein ligase activity / mitotic spindle assembly checkpoint signaling / establishment of mitotic spindle orientation / mitotic sister chromatid segregation / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / APC-Cdc20 mediated degradation of Nek2A / Resolution of Sister Chromatid Cohesion / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / RHO GTPases Activate Formins / negative regulation of protein catabolic process / kinetochore / spindle pole / mitotic spindle / Separation of Sister Chromatids / cell division / perinuclear region of cytoplasm / protein homodimerization activity / nucleoplasm / identical protein binding / nucleus / cytoplasm / cytosol
Similarity search - Function
Cell Cycle, Spindle Assembly Checkpoint Protein; Chain A / HORMA domain / Mad2-like / HORMA domain / HORMA domain / HORMA domain profile. / HORMA domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Mitotic spindle assembly checkpoint protein MAD2A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsLuo, X. / Tang, Z. / Xia, G. / Wassmann, K. / Matsumoto, T. / Rizo, J. / Yu, H.
Citation
Journal: Nat.Struct.Mol.Biol. / Year: 2004
Title: The Mad2 spindle checkpoint protein has two distinct natively folded states.
Authors: Luo, X. / Tang, Z. / Xia, G. / Wassmann, K. / Matsumoto, T. / Rizo, J. / Yu, H.
#1: Journal: Nat.Struct.Biol. / Year: 2000
Title: Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20
Authors: Luo, X. / Fang, G. / Coldiron, M. / Lin, Y. / Yu, H. / Kirschner, M.W. / Wagner, G.
#2: Journal: Mol.Cell / Year: 2002
Title: The Mad2 Spindle Checkpoint Protein Undergoes Similar Major Conformational Changes upon Binding to Either Mad1 or Cdc20
Authors: Luo, X. / Tang, Z. / Rizo, J. / Yu, H.
History
DepositionJan 8, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 30, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 27, 2021Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Mitotic spindle assembly checkpoint protein MAD2A


Theoretical massNumber of molelcules
Total (without water)23,5051
Polymers23,5051
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 500structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Mitotic spindle assembly checkpoint protein MAD2A / MAD2-like 1 / HsMAD2


Mass: 23504.822 Da / Num. of mol.: 1 / Mutation: R133A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MAD2L1, MAD2 / Plasmid: pQE-30 / Production host: Escherichia coli (E. coli) / Strain (production host): M15[pREP4] / References: UniProt: Q13257

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HNCA, HN(CO)CA, HN(CA)CB, HN(COCA)CB
1223D 15N-separated NOESY
1333D 13C-separated NOESY
NMR detailsText: The structure was determined using triple-resonance NMR spectroscopy.

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Sample preparation

Details
Solution-IDContentsSolvent system
10.8mM Mad2 protein U-15N,13C,2H90% H2O, 10% D2O; 50mM phosphate buffer; 0.3M KCl; 1mM DTT
20.8mM Mad2 protein U-15N90% H2O, 10% D2O; 50mM phosphate buffer; 0.3M KCl; 1mM DTT
30.8mM Mad2 protein U-15N,13C90% H2O, 10% D2O; 50mM phosphate buffer; 0.3M KCl; 1mM DTT
Sample conditionsIonic strength: 0.3M KCl / pH: 6.8 / Pressure: ambient / Temperature: 303 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA6001
Varian INOVAVarianINOVA5002

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Processing

NMR software
NameVersionDeveloperClassification
CNS1Brunger, A.T.refinement
NMRPipe1.8Delaglio, F.processing
VNMR6.1Variancollection
NMRView4.1.2Johnson, B.A.data analysis
RefinementMethod: torsion angle dynamics / Software ordinal: 1
Details: The structures are based on a total of 2866 restraints, 2323 are NOE-derived distance constraints, 339 dihedral angle restraints,204 distance restraints from hydrogen bonds.
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 500 / Conformers submitted total number: 1

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