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- PDB-2k94: Structural modification of acyl carrier protein by butyryl group -

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Basic information

Entry
Database: PDB / ID: 2k94
TitleStructural modification of acyl carrier protein by butyryl group
ComponentsAcyl carrier protein
KeywordsLIPID TRANSPORT / Butytyl Form of Acyl Carrier Protein / Fatty Acid Synthesis Protein / Cytoplasm / Fatty acid biosynthesis / Lipid synthesis / Phosphopantetheine
Function / homology
Function and homology information


lipid biosynthetic process / lipid A biosynthetic process / phosphopantetheine binding / acyl binding / acyl carrier activity / fatty acid biosynthetic process / response to xenobiotic stimulus / lipid binding / cytoplasm / cytosol
Similarity search - Function
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
Acyl carrier protein
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsWu, B.N.
CitationJournal: Protein Sci. / Year: 2009
Title: Structural modification of acyl carrier protein by butyryl group.
Authors: Wu, B.N. / Zhang, Y.M. / Rock, C.O. / Zheng, J.J.
History
DepositionSep 29, 2008Deposition site: BMRB / Processing site: RCSB
Revision 1.0Jan 20, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Mar 16, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.3May 22, 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: Acyl carrier protein


Theoretical massNumber of molelcules
Total (without water)8,5131
Polymers8,5131
Non-polymers00
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 #1fewest violations

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Components

#1: Protein Acyl carrier protein / acp / Cytosolic-activating factor / CAF / Fatty acid synthase acyl carrier protein


Mass: 8513.279 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: butyryl form / Source: (gene. exp.) Escherichia coli (E. coli) / Gene: acpP, b1094, JW1080 / Plasmid: pET11a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P0A6A8

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 1H-13C NOESY
1213D 1H-15N NOESY

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Sample preparation

DetailsContents: 1.5 mM [U-100% 13C; U-100% 15N] Butyryl ACP, 40 mM potassium phosphate, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1.5 mMButyryl ACP[U-100% 13C; U-100% 15N]1
40 mMpotassium phosphate1
Sample conditionspH: 6.5 / Temperature units: K

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NMR measurement

NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
DYANAGuntert, Braun and Wuthrichstructure solution
DYANAGuntert, Braun and Wuthrichrefinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 20

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