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- PDB-1klq: The Mad2 Spindle Checkpoint Protein Undergoes Similar Major Confo... -

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Basic information

Entry
Database: PDB / ID: 1klq
TitleThe Mad2 Spindle Checkpoint Protein Undergoes Similar Major Conformational Changes upon Binding to Either Mad1 or Cdc20
Components
  • MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
  • Mad2-binding peptide
KeywordsCELL CYCLE / protein-peptide complex / MAD2 FAMILY
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 ubiquitin protein ligase activity / mitotic spindle assembly checkpoint signaling ...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 ubiquitin protein ligase activity / mitotic spindle assembly checkpoint signaling / mitotic sister chromatid segregation / establishment of mitotic spindle orientation / negative regulation of mitotic cell cycle / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / APC-Cdc20 mediated degradation of Nek2A / RHO GTPases Activate Formins / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / negative regulation of protein catabolic process / mitotic spindle / kinetochore / spindle pole / Separation of Sister Chromatids / cell division / negative regulation of apoptotic process / perinuclear region of cytoplasm / protein homodimerization activity / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
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. / Rizo, J. / Yu, H.
CitationJournal: 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
DepositionDec 12, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 25, 2002Provider: repository / Type: Initial release
Revision 1.1Oct 21, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A
B: Mad2-binding peptide


Theoretical massNumber of molelcules
Total (without water)24,0142
Polymers24,0142
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 100structures with the lowest energy
RepresentativeModel #1the best representative conformer

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Components

#1: Protein MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A / Mad2 / spindle checkpoint protein Mad2 / MAD2-LIKE 1 / HSMAD2 / mitotic feedback control protein Madp2


Mass: 22562.725 Da / Num. of mol.: 1 / Fragment: MISSING N-TERMINAL 10 RESIDUES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pQE-30 / Production host: Escherichia coli (E. coli) / Strain (production host): M15[pREP4] / References: UniProt: Q13257
#2: Protein/peptide Mad2-binding peptide / MBP1


Mass: 1451.604 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: This sequence is identified using phage display

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
222HNCA
3333D 13C-separated NOESY
4443D H(CC)(CO)NH
5553D 15N-separated NOESY
6663D 13C-separated NOESY
272HN(CO)CA
4843D (H)C(C)(CO)NH
292HN(COCA)CB
2102HN(CA)CB
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; 1mM MBP1 NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT90% H2O/10% D2O
20.8mM Mad2 protein U-15N, 13C, 2H; 1mM MBP1 NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT90% H2O/10% D2O
30.8mM Mad2 protein U-15N, 13C; 1mM MBP1 NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT90% H2O/10% D2O
40.8mM Mad2 protein U-15N, 13C, U-60% 2H; 1mM MBP1 NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT90% H2O/10% D2O
50.8mM MBP1 U-15N; 1mM Mad2 protein NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT90% H2O/10% D2O
60.8mM MBP1 U-15N, 13C; 1mM Mad2 protein NA; 50mM phosphate buffer; 0.3M KCl; 1mM DTT90% H2O/10% D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
10.3M KCl 7.4 ambient 303 K
20.3M KCl 7.4 ambient 303 K
30.3M KCl 7.4 ambient 303 K
40.3M KCl 7.4 ambient 303 K
50.3M KCl 7.4 ambient 303 K
60.3M KCl 7.4 ambient 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA5001
Varian INOVAVarianINOVA6002

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Processing

NMR software
NameVersionDeveloperClassification
CNS0.9aBrunger, A.T.structure solution
CNS0.9aBrunger, A.T.refinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
Details: The structures are based on a total of 3124 restraints, 2535 are NOE-derived distance constraints, 363 dihedral angle restraints,226 distance restraints from hydrogen bonds.
NMR representativeSelection criteria: the best representative conformer
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 1

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