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- PDB-2le3: N-terminal regulatory segment of carnitine palmitoyltransferase 1A -

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Basic information

Entry
Database: PDB / ID: 2le3
TitleN-terminal regulatory segment of carnitine palmitoyltransferase 1A
ComponentsCarnitine O-palmitoyltransferase 1, liver isoform
KeywordsTRANSFERASE / membrane protein / amphiphilic structure / membrane-protein interaction / structural switch
Function / homology
Function and homology information


carnitine shuttle / palmitoleoyltransferase activity / carnitine O-palmitoyltransferase / carnitine O-palmitoyltransferase activity / : / regulation of lipid storage / carnitine metabolic process / long-chain fatty acid metabolic process / response to xenobiotic stimulus => GO:0009410 / positive regulation of fatty acid beta-oxidation ...carnitine shuttle / palmitoleoyltransferase activity / carnitine O-palmitoyltransferase / carnitine O-palmitoyltransferase activity / : / regulation of lipid storage / carnitine metabolic process / long-chain fatty acid metabolic process / response to xenobiotic stimulus => GO:0009410 / positive regulation of fatty acid beta-oxidation / Carnitine metabolism / cellular response to fatty acid / Signaling by Retinoic Acid / eating behavior / triglyceride metabolic process / fatty acid beta-oxidation / regulation of insulin secretion / regulation of lipid metabolic process / epithelial cell differentiation / RORA activates gene expression / fatty acid metabolic process / response to organic cyclic compound / PPARA activates gene expression / circadian rhythm / glucose metabolic process / response to ethanol / mitochondrial outer membrane / mitochondrion / membrane / identical protein binding
Similarity search - Function
Carnitine O-palmitoyltransferase, N-terminal / : / Carnitine O-palmitoyltransferase N-terminus / Acyltransferase ChoActase/COT/CPT / Choline/carnitine acyltransferase domain / Choline/Carnitine o-acyltransferase, domain 2 / Choline/Carnitine o-acyltransferase / Acyltransferases ChoActase / COT / CPT family signature 1. / Acyltransferases ChoActase / COT / CPT family signature 2.
Similarity search - Domain/homology
Carnitine O-palmitoyltransferase 1, liver isoform
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model 1
AuthorsUlmer, T.S. / Rao, J.N.
CitationJournal: J.Biol.Chem. / Year: 2011
Title: An Environment-dependent Structural Switch Underlies the Regulation of Carnitine Palmitoyltransferase 1A.
Authors: Rao, J.N. / Warren, G.Z. / Estolt-Povedano, S. / Zammit, V.A. / Ulmer, T.S.
History
DepositionJun 6, 2011Deposition site: BMRB / Processing site: RCSB
Revision 1.0Oct 19, 2011Provider: repository / Type: Initial release
Revision 1.1Dec 28, 2011Group: Database references
Revision 1.2Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer
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
Revision 1.3May 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: Carnitine O-palmitoyltransferase 1, liver isoform


Theoretical massNumber of molelcules
Total (without water)4,8031
Polymers4,8031
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)20 / 20structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Carnitine O-palmitoyltransferase 1, liver isoform / / CPT1-L / Carnitine O-palmitoyltransferase I / liver isoform / CPT I / CPTI-L / Carnitine ...CPT1-L / Carnitine O-palmitoyltransferase I / liver isoform / CPT I / CPTI-L / Carnitine palmitoyltransferase 1A


Mass: 4802.513 Da / Num. of mol.: 1 / Fragment: Cytoplasmic domain residues 1-42
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CPT1A, CPT1 / Production host: Escherichia coli (E. coli)
References: UniProt: P50416, carnitine O-palmitoyltransferase

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D HNCA
1213D HN(CA)CB
131quant j correlation
1413D NOESY

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Sample preparation

DetailsContents: 0.5 mM [U-100% 13C; U-100% 15N; U-80% 2H] protein, 0.5 mM [U-99% 13C; U-99% 15N] protein, 95% H2O/5% D2O
Solvent system: 95% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.5 mMprotein-1[U-100% 13C; U-100% 15N; U-80% 2H]1
0.5 mMprotein-2[U-99% 13C; U-99% 15N]1
Sample conditionsIonic strength: 0.025 / pH: 5.6 / Pressure: ambient / Temperature: 308.2 K

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NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz

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Processing

NMR software
NameDeveloperClassification
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorestructure solution
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorerefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 20 / Conformers submitted total number: 20

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