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- PDB-2ldi: NMR solution structure of ZiaAN sub mutant -

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Basic information

Entry
Database: PDB / ID: 2ldi
TitleNMR solution structure of ZiaAN sub mutant
ComponentsZinc-transporting ATPase
KeywordsHYDROLASE / metal homeostasis / metallochaperones
Function / homology
Function and homology information


P-type Zn2+ transporter / P-type zinc transporter activity / cadmium ion transmembrane transporter activity / zinc ion transport / metal ion transport / transmembrane transport / ATP hydrolysis activity / ATP binding / membrane / metal ion binding / plasma membrane
Similarity search - Function
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, 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
Zinc-transporting ATPase
Similarity search - Component
Biological speciesSynechocystis sp. PCC 6803 substr. Kazusa (bacteria)
MethodSOLUTION NMR / restrained energy minimization
Model detailsfewest violations, model 1
AuthorsBanci, L. / Bertini, I. / Felli, I.C. / Pavelkova, A.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2012
Title: Cyanobacterial metallochaperone inhibits deleterious side reactions of copper.
Authors: Tottey, S. / Patterson, C.J. / Banci, L. / Bertini, I. / Felli, I.C. / Pavelkova, A. / Dainty, S.J. / Pernil, R. / Waldron, K.J. / Foster, A.W. / Robinson, N.J.
History
DepositionMay 26, 2011Deposition site: BMRB / Processing site: RCSB
Revision 1.0Nov 30, 2011Provider: repository / Type: Initial release
Revision 1.1Dec 21, 2011Group: Database references
Revision 1.2Jan 18, 2012Group: Database references
Revision 1.3Apr 27, 2016Group: Structure summary
Revision 1.4Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.5May 15, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Zinc-transporting ATPase


Theoretical massNumber of molelcules
Total (without water)11,4901
Polymers11,4901
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)30 / 300target function
RepresentativeModel #1fewest violations

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Components

#1: Protein Zinc-transporting ATPase / Zn(2+)-translocating P-type ATPase


Mass: 11489.966 Da / Num. of mol.: 1 / Fragment: HMA domain residues 6-111
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Synechocystis sp. PCC 6803 substr. Kazusa (bacteria)
Strain: ATCC 27184 / PCC 6803 / N-1 / Gene: slr0798, ziaA / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta strain / References: UniProt: Q59998, EC: 3.6.3.5

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1213D HNCO
1313D CBCA(CO)NH
1413D HN(CA)CB
1513D (H)CCH-TOCSY
1613D 1H-13C NOESY
1713D 1H-15N NOESY

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Sample preparation

DetailsContents: 0.5 mM [U-99% 13C; U-99% 15N] ZiaAN sub, 50 mM sodium phosphate, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.5 mMZiaAN sub-1[U-99% 13C; U-99% 15N]1
50 mMsodium phosphate-21
Sample conditionsIonic strength: 50 / pH: 7.00 / Pressure: 1 atm / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE5001
Bruker AvanceBrukerAVANCE7002
Bruker AvanceBrukerAVANCE8003

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Processing

NMR software
NameVersionDeveloperClassification
TopSpin2Bruker Biospincollection
AmberCase, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, and Kollmrefinement
RefinementMethod: restrained energy minimization / Software ordinal: 1
NMR constraintsNOE constraints total: 761 / NOE intraresidue total count: 128 / NOE long range total count: 269 / NOE medium range total count: 168 / NOE sequential total count: 196
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 300 / Conformers submitted total number: 30

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