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- PDB-6nuu: Structure of Calcineurin mutant in complex with NHE1 peptide -

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Basic information

Entry
Database: PDB / ID: 6nuu
TitleStructure of Calcineurin mutant in complex with NHE1 peptide
Components
  • Calcineurin subunit B type 1
  • Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
  • Sodium/hydrogen exchanger 1
KeywordsHYDROLASE/Calcium Binding Protein / Ser/thr phosphatase / complex / HYDROLASE / HYDROLASE-Calcium Binding Protein complex
Function / homology
Function and homology information


Sodium/Proton exchangers / negative regulation of angiotensin-activated signaling pathway / calcium-dependent protein serine/threonine phosphatase regulator activity / regulation of cell proliferation involved in kidney morphogenesis / regulation of the force of heart contraction by cardiac conduction / positive regulation of glomerulus development / negative regulation of calcium ion import across plasma membrane / cation-transporting ATPase complex / negative regulation of signaling / calcium-dependent protein serine/threonine phosphatase activity ...Sodium/Proton exchangers / negative regulation of angiotensin-activated signaling pathway / calcium-dependent protein serine/threonine phosphatase regulator activity / regulation of cell proliferation involved in kidney morphogenesis / regulation of the force of heart contraction by cardiac conduction / positive regulation of glomerulus development / negative regulation of calcium ion import across plasma membrane / cation-transporting ATPase complex / negative regulation of signaling / calcium-dependent protein serine/threonine phosphatase activity / protein serine/threonine phosphatase complex / Hyaluronan degradation / positive regulation of saliva secretion / peptidyl-serine dephosphorylation / calmodulin-dependent protein phosphatase activity / regulation of cardiac muscle cell membrane potential / calcineurin complex / positive regulation of calcium ion-dependent exocytosis of neurotransmitter / positive regulation of connective tissue replacement / positive regulation of calcium ion import across plasma membrane / cellular response to electrical stimulus / negative regulation of dendrite morphogenesis / positive regulation of cardiac muscle hypertrophy in response to stress / potassium:proton antiporter activity / renal filtration / positive regulation of action potential / lung epithelial cell differentiation / sodium:proton antiporter activity / calcineurin-NFAT signaling cascade / maintenance of cell polarity / regulation of pH / positive regulation of calcineurin-NFAT signaling cascade / cardiac muscle cell differentiation / sodium ion export across plasma membrane / protein phosphatase 2B binding / transition between fast and slow fiber / skeletal muscle tissue regeneration / myelination in peripheral nervous system / intracellular sodium ion homeostasis / regulation of stress fiber assembly / positive regulation of osteoclast differentiation / cardiac muscle hypertrophy in response to stress / cardiac muscle cell contraction / regulation of synaptic vesicle cycle / sodium ion import across plasma membrane / positive regulation of mitochondrial membrane permeability / dephosphorylation / response to acidic pH / regulation of cardiac muscle contraction by calcium ion signaling / cellular response to acidic pH / regulation of focal adhesion assembly / extrinsic component of plasma membrane / branching involved in blood vessel morphogenesis / dendrite morphogenesis / protein dephosphorylation / protein-serine/threonine phosphatase / CLEC7A (Dectin-1) induces NFAT activation / regulation of postsynaptic neurotransmitter receptor internalization / cellular response to cold / positive regulation of cardiac muscle hypertrophy / cellular response to antibiotic / positive regulation of the force of heart contraction / protein serine/threonine phosphatase activity / parallel fiber to Purkinje cell synapse / calcineurin-mediated signaling / protein complex oligomerization / positive regulation of activated T cell proliferation / intercalated disc / epithelial to mesenchymal transition / Calcineurin activates NFAT / positive regulation of endocytosis / epidermis development / Activation of BAD and translocation to mitochondria / DARPP-32 events / positive regulation of osteoblast differentiation / multicellular organismal response to stress / phosphatase binding / postsynaptic modulation of chemical synaptic transmission / keratinocyte differentiation / skeletal muscle fiber development / response to muscle stretch / phosphatidylinositol-4,5-bisphosphate binding / monoatomic ion transport / potassium ion transmembrane transport / cellular response to epinephrine stimulus / T-tubule / FCERI mediated Ca+2 mobilization / proton transmembrane transport / positive regulation of cell adhesion / T cell activation / stem cell differentiation / hippocampal mossy fiber to CA3 synapse / regulation of intracellular pH / excitatory postsynaptic potential / wound healing / cellular response to mechanical stimulus / G1/S transition of mitotic cell cycle / response to calcium ion / sarcolemma / phospholipid binding
Similarity search - Function
Sodium/hydrogen exchanger 1-like / Sodium/hydrogen exchanger, regulatory region / Regulatory region of Na+/H+ exchanger NHE binds to calmodulin / Na+/H+ exchanger / PP2B, metallophosphatase domain / PP2B / Cation/H+ exchanger, CPA1 family / Cation/H+ exchanger / Sodium/hydrogen exchanger, transmembrane / Serine/threonine specific protein phosphatases signature. ...Sodium/hydrogen exchanger 1-like / Sodium/hydrogen exchanger, regulatory region / Regulatory region of Na+/H+ exchanger NHE binds to calmodulin / Na+/H+ exchanger / PP2B, metallophosphatase domain / PP2B / Cation/H+ exchanger, CPA1 family / Cation/H+ exchanger / Sodium/hydrogen exchanger, transmembrane / Serine/threonine specific protein phosphatases signature. / Protein phosphatase 2A homologues, catalytic domain. / Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase / Metallo-dependent phosphatases / Purple Acid Phosphatase; chain A, domain 2 / Calcineurin-like phosphoesterase domain, ApaH type / Calcineurin-like phosphoesterase / Metallo-dependent phosphatase-like / EF-hand / Recoverin; domain 1 / EF-hand domain pair / EF-hand, calcium binding motif / EF-Hand 1, calcium-binding site / EF-hand calcium-binding domain. / EF-hand calcium-binding domain profile. / EF-hand domain / 4-Layer Sandwich / EF-hand domain pair / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
: / DI(HYDROXYETHYL)ETHER / PHOSPHATE ION / Sodium/hydrogen exchanger 1 / Calcineurin subunit B type 1 / Protein phosphatase 3 catalytic subunit alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsWang, X. / Page, R. / Peti, W.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)R01NS091336 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM098482 United States
CitationJournal: Nat Commun / Year: 2019
Title: Molecular basis for the binding and selective dephosphorylation of Na+/H+exchanger 1 by calcineurin.
Authors: Hendus-Altenburger, R. / Wang, X. / Sjogaard-Frich, L.M. / Pedraz-Cuesta, E. / Sheftic, S.R. / Bendsoe, A.H. / Page, R. / Kragelund, B.B. / Pedersen, S.F. / Peti, W.
History
DepositionFeb 2, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 3, 2019Provider: repository / Type: Initial release
Revision 1.1Aug 21, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Dec 18, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Oct 11, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform
B: Calcineurin subunit B type 1
C: Sodium/hydrogen exchanger 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,20211
Polymers65,7193
Non-polymers4838
Water4,612256
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: isothermal titration calorimetry
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7420 Å2
ΔGint-154 kcal/mol
Surface area22480 Å2
MethodPISA
Unit cell
Length a, b, c (Å)79.303, 125.966, 127.352
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11A-542-

HOH

21A-693-

HOH

31A-696-

HOH

41A-697-

HOH

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Components

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Protein , 2 types, 2 molecules AB

#1: Protein Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform / CAM-PRP catalytic subunit / Calmodulin-dependent calcineurin A subunit alpha isoform


Mass: 42695.883 Da / Num. of mol.: 1 / Mutation: H155A, Y159A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PPP3CA, CALNA, CNA / Production host: Escherichia coli (E. coli)
References: UniProt: Q08209, protein-serine/threonine phosphatase
#2: Protein Calcineurin subunit B type 1 / Protein phosphatase 2B regulatory subunit 1 / Protein phosphatase 3 regulatory subunit B alpha isoform 1


Mass: 17755.174 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PPP3R1, CNA2, CNB / Production host: Escherichia coli (E. coli) / References: UniProt: P63098

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Protein/peptide , 1 types, 1 molecules C

#3: Protein/peptide Sodium/hydrogen exchanger 1 / APNH / Na(+)/H(+) antiporter / amiloride-sensitive / Na(+)/H(+) exchanger 1 / NHE-1 / Solute ...APNH / Na(+)/H(+) antiporter / amiloride-sensitive / Na(+)/H(+) exchanger 1 / NHE-1 / Solute carrier family 9 member 1


Mass: 5268.008 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SLC9A1, APNH1, NHE1 / Production host: Escherichia coli (E. coli) / References: UniProt: P19634

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Non-polymers , 6 types, 264 molecules

#4: Chemical ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe
#5: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#6: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4
#7: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#8: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 256 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.49 Å3/Da / Density % sol: 50.6 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 9.5
Details: 40% (v/v) PEG 600, 100 mM CHES/ Sodium hydroxide pH 9.5, 0.2 M MgCl2

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: LIQUID ANODE / Type: BRUKER METALJET / Wavelength: 1.34 Å
DetectorType: Bruker PHOTON II / Detector: PIXEL / Date: Nov 18, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.34 Å / Relative weight: 1
ReflectionResolution: 2.3→20.8 Å / Num. obs: 28153 / % possible obs: 99.8 % / Redundancy: 5.3 % / CC1/2: 0.984 / Net I/σ(I): 5.9
Reflection shellResolution: 2.3→2.38 Å / Num. unique obs: 14368 / CC1/2: 0.714

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
SAINTdata reduction
SADABSdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5SVE

5sve


Resolution: 2.3→20.8 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 24.69
RfactorNum. reflection% reflection
Rfree0.243 1907 6.98 %
Rwork0.195 --
obs0.198 27309 95.3 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.3→20.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4274 0 18 256 4548
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0064399
X-RAY DIFFRACTIONf_angle_d0.695958
X-RAY DIFFRACTIONf_dihedral_angle_d13.612639
X-RAY DIFFRACTIONf_chiral_restr0.044653
X-RAY DIFFRACTIONf_plane_restr0.005780
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3001-2.35750.35761270.27931690X-RAY DIFFRACTION90
2.3575-2.42120.36091260.27251712X-RAY DIFFRACTION91
2.4212-2.49230.28681250.25521709X-RAY DIFFRACTION90
2.4923-2.57260.3121370.24351727X-RAY DIFFRACTION92
2.5726-2.66440.30641320.23081766X-RAY DIFFRACTION94
2.6644-2.77080.2511370.21721795X-RAY DIFFRACTION96
2.7708-2.89660.24151300.21291815X-RAY DIFFRACTION96
2.8966-3.04890.25061330.21321834X-RAY DIFFRACTION96
3.0489-3.23930.27751420.20661828X-RAY DIFFRACTION97
3.2393-3.48830.22351390.20551837X-RAY DIFFRACTION97
3.4883-3.83740.22271420.17011834X-RAY DIFFRACTION96
3.8374-4.38820.19761440.14111923X-RAY DIFFRACTION99
4.3882-5.51180.18761390.14721919X-RAY DIFFRACTION99
5.5118-20.90010.19791540.16952013X-RAY DIFFRACTION100

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