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- PDB-1y8m: Solution Structure of Yeast Mitochondria Fission Protein Fis1 -

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Basic information

Entry
Database: PDB / ID: 1y8m
TitleSolution Structure of Yeast Mitochondria Fission Protein Fis1
ComponentsFis1
KeywordsUNKNOWN FUNCTION / Mitochondria / Fission
Function / homology
Function and homology information


Class I peroxisomal membrane protein import / peroxisome organization / peroxisome fission / mitochondrial fission / positive regulation of mitochondrial fission / peroxisome / mitochondrial outer membrane / apoptotic process / mitochondrion
Similarity search - Function
Mitochondria fission 1 protein / Fis1, N-terminal tetratricopeptide repeat / Fis1, C-terminal tetratricopeptide repeat / Mitochondria fission protein Fis1, cytosolic domain / Fis1 N-terminal tetratricopeptide repeat / Fis1 C-terminal tetratricopeptide repeat / Tetratricopeptide repeat domain / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Tetratricopeptide-like helical domain superfamily / Mainly Alpha
Similarity search - Domain/homology
Mitochondrial fission 1 protein
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING, MOLECULAR DYNAMICS
AuthorsSuzuki, M. / Youle, R.J. / Tjandra, N.
CitationJournal: J.Biol.Chem. / Year: 2005
Title: Novel structure of the N terminus in yeast Fis1 correlates with a specialized function in mitochondrial fission.
Authors: Suzuki, M. / Neutzner, A. / Tjandra, N. / Youle, R.J.
History
DepositionDec 13, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 5, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Fis1


Theoretical massNumber of molelcules
Total (without water)16,7251
Polymers16,7251
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)20 / 100structures with the lowest energy
RepresentativeModel #1

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Components

#1: Protein Fis1 /


Mass: 16725.078 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Plasmid: pET21 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P40515

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-separated NOESY
1224D 13C/15N-separated NOESY
1334D 13C-separated NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
11mM Protein U-15N90% H2O/10% D2O
21mM Protein U-15N, 13C90% H2O/10% D2O
31mM Protein U-15N, 13C100% D2O
Sample conditionsIonic strength: 10 mM Tris Acetate / pH: 5.5 / Pressure: AMBIENT / Temperature: 305 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
Bruker DRXBrukerDRX6001
Bruker DRXBrukerDRX8002

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Processing

NMR software
NameVersionClassification
XwinNMR3.1collection
NMRPipe2.3processing
PIPP4.2.8data analysis
XPLOR-NIH3.8.5structure solution
XPLOR-NIH3.8.5refinement
RefinementMethod: DISTANCE GEOMETRY, SIMULATED ANNEALING, MOLECULAR DYNAMICS
Software ordinal: 1
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20

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