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- PDB-1ev0: SOLUTION STRUCTURE OF THE MINE TOPOLOGICAL SPECIFICITY DOMAIN -

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Basic information

Entry
Database: PDB / ID: 1ev0
TitleSOLUTION STRUCTURE OF THE MINE TOPOLOGICAL SPECIFICITY DOMAIN
ComponentsMINE
KeywordsCELL CYCLE / MinE / topological specificity / cell division / MinCD / minicell
Function / homology
Function and homology information


division septum site selection / regulation of division septum assembly / regulation of cell division / identical protein binding / plasma membrane / cytosol
Similarity search - Function
Cell division topological specificity factor MinE / Cell Cycle; Chain A / Cell division topological specificity factor MinE superfamily / Septum formation topological specificity factor MinE / Cell division topological specificity factor MinE / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Cell division topological specificity factor
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / torsion angle dynamics, dynamical simulated annealing
AuthorsKing, G.F. / Maciejewski, M.W. / Pan, B. / Mullen, G.P.
Citation
Journal: Nat.Struct.Biol. / Year: 2000
Title: Structural basis for the topological specificity function of MinE.
Authors: King, G.F. / Shih, Y.L. / Maciejewski, M.W. / Bains, N.P. / Pan, B. / Rowland, S.L. / Mullen, G.P. / Rothfield, L.I.
#1: Journal: Cell(Cambridge,Mass.) / Year: 1989
Title: A Division Inhibitor and a Topological Specificity Factor Coded for by the Minicell Locus Determine Proper Placement of the Division Septum in E. coli
Authors: de Boer, P.A.J. / Crossley, R.E. / Rothfield, L.I.
#2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1995
Title: Proper Placement of the Escherichia coli Division Site Requires Two Functions that are Associated with Different Domains of the MinE Protein
Authors: Zhao, C.R. / de Boer, P.A.J. / Rothfield, L.I.
#3: Journal: Cell(Cambridge,Mass.) / Year: 1997
Title: The MinE ring: An FtsZ-Independent Cell Structure Required for Selection of the Correct Division Site in E. coli
Authors: Raskin, D.M. / de Boer, P.A.J.
#4: Journal: MOL.MICROBIOL. / Year: 1999
Title: The Dimerization and Topological Specificity Functions of MinE Reside in a Structurally Autonomous C-terminal Domain
Authors: King, G.F. / Rowland, S.L. / Pan, B. / Mackay, J.P. / Mullen, G.P. / Rothfield, L.I.
History
DepositionApr 19, 2000Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 1, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
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: MINE
B: MINE


Theoretical massNumber of molelcules
Total (without water)13,4272
Polymers13,4272
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 / 60Lowest energy and least restraint violations
RepresentativeModel #1lowest energy

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Components

#1: Protein MINE / CELL DIVISION TOPOLOGICAL SPECIFICITY FACTOR


Mass: 6713.656 Da / Num. of mol.: 2 / Fragment: MINE TOPOLOGICAL SPECIFICITY DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET15B / Production host: Escherichia coli (E. coli) / References: UniProt: P0A734

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
1213D HNHA and 3D HNHB
1312D HMQC-J
1413D 15N-separated TOCSY
1543D 13C-separated NOESY
1623D CBCA(CO)NH and 3D HN(CA)CB
1723D HNCO
1843D (H)CCH-TOCSY
1923D C(CO)NH TOCSY and 3D HC(CO)NH TOCSY
110313C and 15N 3D edited/filtered NOESY
NMR detailsText: The structure was determined using triple-resonance NMR spectroscopy. Intermonomer NOEs were determined using a heterolabeled protein sample.

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Sample preparation

Details
Solution-IDContentsSolvent system
13.0 mM U-15N,13C MinE; 20 mM sodium phosphate; 50 mM NaCl; 15 mM DTT; 1 mM EDTA; 0.02% sodium azide; 1 mM 4-(2-aminoethyl)benzenesulfonyl fluoride; pH 5.792.5% H2O, 7.5% D2O
23.5 mM U-15N MinE; 20 mM sodium phosphate; 50 mM NaCl; 15 mM DTT; 1 mM EDTA; 0.02% sodium azide; 1 mM 4-(2-aminoethyl)benzenesulfonyl fluoride; pH 5.792.5% H2O, 7.5% D2O
32.13 mM unlabeled MinE; 2.06 mM U-15N,13C MinE; 20 mM sodium phosphate; 50 mM NaCl; 15 mM DTT; 1.5 mM EDTA; 0.02% sodium azide; 0.2 mM PMSF; pH 5.795% H2O/5% D2O
43.0 mM U-15N,13C MinE; 20 mM sodium phosphate; 50 mM NaCl; 15 mM DTT; 1.5 mM EDTA; 0.02% sodium azide; 0.2 mM PMSF; pH 5.7100% D2O
Sample conditionsIonic strength: 0.075 / pH: 5.7 / Pressure: ambient / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA6001
Varian INOVAVarianINOVA5002

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Processing

NMR software
NameVersionDeveloperClassification
Felix97Molecular Simulationsprocessing
XEASY1.3.13Tai-he Xia and Christian Bartelsdata analysis
DYANA1.5Peter Guentertstructure solution
X-PLOR3.851Axel Brungerrefinement
RefinementMethod: torsion angle dynamics, dynamical simulated annealing
Software ordinal: 1
Details: 900 structures were calculated using torsion angle dynamics (DYANA). The best 60 structures were then refined using dynamical simulated annealing in X-PLOR.
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: Lowest energy and least restraint violations
Conformers calculated total number: 60 / Conformers submitted total number: 20

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