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- PDB-1tl4: Solution structure of Cu(I) HAH1 -

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Basic information

Entry
Database: PDB / ID: 1tl4
TitleSolution structure of Cu(I) HAH1
ComponentsCopper transport protein ATOX1
KeywordsMETAL TRANSPORT / copper protein / copper chaperone / Menkes / Wilson / Structural Proteomics in Europe / SPINE / Structural Genomics
Function / homology
Function and homology information


metallochaperone activity / Ion influx/efflux at host-pathogen interface / copper-dependent protein binding / copper chaperone activity / copper ion export / copper ion transport / cuprous ion binding / Detoxification of Reactive Oxygen Species / cellular copper ion homeostasis / response to oxidative stress ...metallochaperone activity / Ion influx/efflux at host-pathogen interface / copper-dependent protein binding / copper chaperone activity / copper ion export / copper ion transport / cuprous ion binding / Detoxification of Reactive Oxygen Species / cellular copper ion homeostasis / response to oxidative stress / ATPase binding / copper ion binding / negative regulation of apoptotic process / cytosol
Similarity search - Function
Heavy-metal-associated domain. / Heavy-metal-associated, conserved site / Heavy-metal-associated domain / Heavy-metal-associated domain profile. / Heavy metal-associated domain superfamily / Heavy metal-associated domain, HMA / Alpha-Beta Plaits - #100 / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
COPPER (I) ION / Copper transport protein ATOX1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics, simulated annealing, restrained energy minimization
AuthorsAnastassopoulou, I. / Banci, L. / Bertini, I. / Cantini, F. / Katsari, E. / Rosato, A. / Structural Proteomics in Europe (SPINE)
CitationJournal: Biochemistry / Year: 2004
Title: Solution Structure of the Apo and Copper(I)-Loaded Human Metallochaperone HAH1.
Authors: Anastassopoulou, I. / Banci, L. / Bertini, I. / Cantini, F. / Katsari, E. / Rosato, A.
History
DepositionJun 9, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 26, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Copper transport protein ATOX1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)7,4762
Polymers7,4131
Non-polymers641
Water0
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)30 / 400target function
Representative

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Components

#1: Protein Copper transport protein ATOX1 / Metal transport protein ATX1


Mass: 7412.646 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ATOX1, HAH1 / Plasmid: pET20b+ / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: O00244
#2: Chemical ChemComp-CU1 / COPPER (I) ION / Copper


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
212CBCANH
222CBCA(CO)NH
232HNCO
242HN(CA)CO
252(H)CCH TOCSY
262HNHA
1713D 15N-separated NOESY
1812D NOESY
1912D TOCSY
21023D 13C-separated NOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
11.0 mM Cu(I)HAH1 U-15N; 10 mM sodium acetate90% H2O/10% D2O
22 mM Cu(I)HAH1 U-95% 13C,U-98% 15N; 4 mM DTT; 100 mM phosphate buffer90% H2O/10% D2O
Sample conditions
Conditions-IDIonic strengthpHPressure (Pa)Temperature (K)
110 mM sodium acetate 6 ambient 298 K
2100 mM phosphate buffer 7 ambient 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 AvanceBrukerAvance5001
Bruker AvanceBrukerAvance9002
Bruker AvanceBrukerAvance6003

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Processing

NMR software
NameVersionClassification
XWINNMRcollection
XEASY1.3data analysis
DIANA1.5structure solution
CYANA1structure solution
AMBER5refinement
RefinementMethod: torsion angle dynamics, simulated annealing, restrained energy minimization
Software ordinal: 1
Details: the structures were based on a total of 1219 meaningful distance constraints, 99 dihedral angle restraints.
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 400 / Conformers submitted total number: 30

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