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- PDB-1jo6: Solution structure of the cytoplasmic N-terminus of the BK beta-s... -

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Basic information

Entry
Database: PDB / ID: 1jo6
TitleSolution structure of the cytoplasmic N-terminus of the BK beta-subunit KCNMB2
Componentspotassium large conductance calcium-activated channel, subfamily M, beta member 2
KeywordsMETAL TRANSPORT / MEMBRANE PROTEIN / helix / ion channel / cytoplasmic part of
Function / homology
Function and homology information


Ca2+ activated K+ channels / calcium-activated potassium channel activity / ion channel inhibitor activity / cGMP effects / action potential / detection of calcium ion / potassium channel regulator activity / regulation of vasoconstriction / neuronal action potential / voltage-gated potassium channel complex ...Ca2+ activated K+ channels / calcium-activated potassium channel activity / ion channel inhibitor activity / cGMP effects / action potential / detection of calcium ion / potassium channel regulator activity / regulation of vasoconstriction / neuronal action potential / voltage-gated potassium channel complex / potassium ion transport / plasma membrane
Similarity search - Function
KCNMB2, ball/chain domain / KCNMB2, ball/chain domain / KCNMB2, ball/chain domain superfamily / KCNMB2, ball and chain domain / Potassium channel, calcium-activated, BK, beta subunit / Calcium-activated potassium channel, beta subunit / Cytochrome C Oxidase; Chain M / Few Secondary Structures / Irregular
Similarity search - Domain/homology
Calcium-activated potassium channel subunit beta-2
Similarity search - Component
MethodSOLUTION NMR / simulated annealing, torsion angle dynamics
AuthorsBentrop, D. / Beyermann, M. / Wissmann, R. / Fakler, B.
Citation
Journal: J.Biol.Chem. / Year: 2001
Title: NMR structure of the "ball-and-chain" domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels.
Authors: Bentrop, D. / Beyermann, M. / Wissmann, R. / Fakler, B.
#1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1999
Title: Molecular basis of fast inactivation in voltage and Ca2+-activated K+ channels: a transmembrane beta-subunit homolog
Authors: Wallner, M. / Meera, P. / Toro, L.
#2: Journal: J.Neurosci. / Year: 1999
Title: Molecular basis for the inactivation of Ca2+- and voltage-dependent BK channels in adrenal chromaffin cells and rat insulinoma tumor cells
Authors: Xia, X.M. / Ding, J.P. / Lingle, C.J.
History
DepositionJul 27, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 16, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: potassium large conductance calcium-activated channel, subfamily M, beta member 2


Theoretical massNumber of molelcules
Total (without water)5,3801
Polymers5,3801
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)24 / 30structures with the least restraint violations,target function
RepresentativeModel #1fewest violations

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Components

#1: Protein/peptide potassium large conductance calcium-activated channel, subfamily M, beta member 2 / KCNMB2 / MaxiK channel beta 2 subunit / large conductance calcium-activated potassium channel beta2 subunit


Mass: 5380.064 Da / Num. of mol.: 1 / Fragment: cytoplasmic N-terminus of KCNMB2, residues 1-45 / Source method: obtained synthetically
Details: The 45-residue peptide was synthesized by standard solid-phase synthesis. The sequence occurs naturally in humans.
References: UniProt: Q9Y691

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1111H-1H NOESY (2D)
121DQF-COSY
1321H-1H NOESY (2D)
NMR detailsText: The structure was determined using standard 2D homonuclear techniques

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Sample preparation

Details
Solution-IDContentsSolvent system
12mM KCNMB2(residues 1-45), NA; 90% H2O, 10% D2O90% H2O/10% D2O
22mM KCNMB2(residues 1-45), NA; 99.9% D2O99.9% D2O
Sample conditionsIonic strength: 0 / pH: 3 / Pressure: ambient / Temperature: 288 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.6Brukercollection
AURELIA2.7.5Neidigdata analysis
XEASY1.3.13Bartelsdata analysis
DYANA1.5Mumenthaler, Guentertrefinement
RefinementMethod: simulated annealing, torsion angle dynamics / Software ordinal: 1
Details: The structures are based on 728 NOE-derived distance constraints (486 intraresidual, 191 sequential, 51 medium-range), 5 dihedral angle restraints, 11 stereospecific assignments
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: structures with the least restraint violations,target function
Conformers calculated total number: 30 / Conformers submitted total number: 24

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