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- PDB-2fq0: Solution structure of major conformation of holo-acyl carrier pro... -

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Basic information

Entry
Database: PDB / ID: 2fq0
TitleSolution structure of major conformation of holo-acyl carrier protein from malaria parasite plasmodium falciparum
Componentsacyl carrier protein
KeywordsLIPID TRANSPORT / HOLO-PFACP / 4'-PHOSPHOPANTETHEINE
Function / homology
Function and homology information


acyl carrier activity
Similarity search - Function
Acyl carrier protein, chloroplastic / ACP-like / Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A / Acyl carrier protein (ACP) / Phosphopantetheine attachment site / Phosphopantetheine attachment site. / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain ...Acyl carrier protein, chloroplastic / ACP-like / Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A / Acyl carrier protein (ACP) / Phosphopantetheine attachment site / Phosphopantetheine attachment site. / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
4'-PHOSPHOPANTETHEINE / Acyl carrier protein
Similarity search - Component
Biological speciesPlasmodium falciparum (malaria parasite P. falciparum)
MethodSOLUTION NMR / TORSION ANGLE DYNAMICS, SIMULATED ANNEALING
AuthorsSharma, A.K. / Sharma, S.K. / Surolia, A. / Surolia, N. / Sarma, S.P.
CitationJournal: Biochemistry / Year: 2006
Title: Solution structures of conformationally equilibrium forms of holo-acyl carrier protein (PfACP) from Plasmodium falciparum provides insight into the mechanism of activation of ACPs
Authors: Sharma, A.K. / Sharma, S.K. / Surolia, A. / Surolia, N. / Sarma, S.P.
History
DepositionJan 17, 2006Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Aug 8, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Source and taxonomy / Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: acyl carrier protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)9,3752
Polymers9,0161
Non-polymers3581
Water0
1


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

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Components

#1: Protein acyl carrier protein /


Mass: 9016.169 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum)
Strain: 3D7 / Gene: malaria parasite P. falciparum / Plasmid: PET-28A(+) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O77077
#2: Chemical ChemComp-PNS / 4'-PHOSPHOPANTETHEINE / Phosphopantetheine


Mass: 358.348 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H23N2O7PS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-SEPARATED NOESY
1213D 13C-separated NOESY
1312D NOESY
1412D TOCSY
151HNHA
161HN(CA)CB, CBCA(CO)NH, H(CCO)NH, C(CCO)NH, HNCO, (H)CCH-TOCSY, 1H-15N HSQC, 1H-13C HSQC
NMR detailsText: Structures are based on 1226 noe derived distance constraints, 55 dihedral restraints and 26 distance restraints from hydrogen bonds

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Sample preparation

DetailsContents: 1.2-1.4mM PFACP U-15N ,13C; 50MM PHOSPHATE BUFFER, 100MM NaCl; PH 6.5, 2MM DTT, 0.5% NAN3
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 50mM PHOSPHATE BUFFER IN 100mM NaCl / pH: 6.5 / Pressure: AMBIENT / Temperature: 300 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAvance7001
Varian INOVAVarianINOVA5002

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Processing

NMR software
NameVersionDeveloperClassification
NMRPipe97.027.12.56Frank Delaglioprocessing
ANSIG1.0.3P. Kraulisdata analysis
CYANA2.1Peter Guntertstructure solution
CYANA2.1Peter Guntertrefinement
RefinementMethod: TORSION ANGLE DYNAMICS, SIMULATED ANNEALING / Software ordinal: 1
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 20 / Conformers submitted total number: 20

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