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- PDB-2ggp: Solution structure of the Atx1-Cu(I)-Ccc2a complex -

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Basic information

Entry
Database: PDB / ID: 2ggp
TitleSolution structure of the Atx1-Cu(I)-Ccc2a complex
Components
  • Metal homeostasis factor ATX1
  • Probable copper-transporting ATPase
KeywordsCHAPERONE / METAL TRANSPORT / Copper transport / complex / Structural Genomics / Structural Proteomics in Europe / SPINE
Function / homology
Function and homology information


trans-Golgi network transport vesicle membrane / copper chaperone activity / Ion transport by P-type ATPases / P-type divalent copper transporter activity / P-type monovalent copper transporter activity / P-type Cu+ transporter / copper ion export / copper ion import / copper ion homeostasis / copper ion transport ...trans-Golgi network transport vesicle membrane / copper chaperone activity / Ion transport by P-type ATPases / P-type divalent copper transporter activity / P-type monovalent copper transporter activity / P-type Cu+ transporter / copper ion export / copper ion import / copper ion homeostasis / copper ion transport / ATPase-coupled monoatomic cation transmembrane transporter activity / intracellular copper ion homeostasis / trans-Golgi network / transmembrane transport / cellular response to oxidative stress / intracellular iron ion homeostasis / copper ion binding / ATP hydrolysis activity / ATP binding / membrane / metal ion binding / plasma membrane / cytosol
Similarity search - Function
Heavy metal-associated domain, copper ion-binding / P-type ATPase, subfamily IB / Heavy-metal-associated, conserved site / Heavy-metal-associated domain. / Heavy-metal-associated domain / Heavy metal-associated domain superfamily / Heavy-metal-associated domain profile. / Heavy metal-associated domain, HMA / Alpha-Beta Plaits - #100 / E1-E2 ATPase ...Heavy metal-associated domain, copper ion-binding / P-type ATPase, subfamily IB / Heavy-metal-associated, conserved site / Heavy-metal-associated domain. / Heavy-metal-associated domain / Heavy metal-associated domain superfamily / Heavy-metal-associated domain profile. / Heavy metal-associated domain, HMA / Alpha-Beta Plaits - #100 / E1-E2 ATPase / P-type ATPase, haloacid dehalogenase domain / P-type ATPase, phosphorylation site / P-type ATPase, cytoplasmic domain N / E1-E2 ATPases phosphorylation site. / P-type ATPase, A domain superfamily / P-type ATPase / P-type ATPase, transmembrane domain superfamily / haloacid dehalogenase-like hydrolase / HAD superfamily / HAD-like superfamily / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
COPPER (I) ION / Copper chaperone ATX1 / Copper-transporting ATPase
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodSOLUTION NMR
AuthorsBanci, L. / Bertini, I. / Cantini, F. / Felli, I.C. / Gonnelli, L. / Hadjiliadis, N. / Pierattelli, R. / Rosato, A. / Voulgaris, P. / Structural Proteomics in Europe (SPINE)
CitationJournal: Nat.Chem.Biol. / Year: 2006
Title: The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction.
Authors: Banci, L. / Bertini, I. / Cantini, F. / Felli, I.C. / Gonnelli, L. / Hadjiliadis, N. / Pierattelli, R. / Rosato, A. / Voulgaris, P.
History
DepositionMar 24, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 8, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 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 / struct_conn / struct_ref_seq_dif / struct_site
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 / _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 / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4May 29, 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: Metal homeostasis factor ATX1
B: Probable copper-transporting ATPase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)16,1863
Polymers16,1232
Non-polymers641
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 200target function
RepresentativeModel #1lowest energy

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Components

#1: Protein Metal homeostasis factor ATX1


Mass: 8232.650 Da / Num. of mol.: 1 / Fragment: HMA domain, residues 1-73
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: ATX1 / Plasmid: PET11D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P38636
#2: Protein Probable copper-transporting ATPase / Cu2+ / -ATPase


Mass: 7889.924 Da / Num. of mol.: 1 / Fragment: HMA 1 domain, residues 2-72
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: CCC2 / Plasmid: PET11D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P38995, Cu2+-exporting ATPase
#3: Chemical ChemComp-CU1 / COPPER (I) ION


Mass: 63.546 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cu

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1212D TOCSY
1312D 15N edited NOESY
1412D 13C edited NOESY
1512D 13C filtered NOESY
161NOESY for intermolecular NOEs

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Sample preparation

DetailsContents: 1mM Atx1 U-15N,13C, 1mM Ccc2a unlabeled, 1mM Cu(I), 100mM KPi, 90% H2O, 10% D2O
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 100 mM KPi / pH: 7.0 / Pressure: ambient / Temperature: 298 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 AVANCEBrukerAVANCE8001
Bruker AVANCEBrukerAVANCE5002

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Processing

NMR software
NameVersionDeveloperClassification
DYANA1.5Guentert, P., Mumenthaler, C., and Wuthrich, K.structure solution
Amber8Case, D.A. et al.refinement
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20

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