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- PDB-2m76: Structure of the Regulatory Domain of Human Brain Carnitine Palmi... -

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Basic information

Entry
Database: PDB / ID: 2m76
TitleStructure of the Regulatory Domain of Human Brain Carnitine Palmitoyltransferase 1
ComponentsCarnitine O-palmitoyltransferase 1, brain isoform
KeywordsSIGNALING PROTEIN / acyl transfer / carnitine / malonyl-coenzyme A
Function / homology
Function and homology information


carnitine O-palmitoyltransferase / carnitine O-palmitoyltransferase activity / carnitine metabolic process / fatty acid beta-oxidation / AMPA glutamate receptor complex / fatty acid metabolic process / mitochondrial outer membrane / axon / synapse / dendrite ...carnitine O-palmitoyltransferase / carnitine O-palmitoyltransferase activity / carnitine metabolic process / fatty acid beta-oxidation / AMPA glutamate receptor complex / fatty acid metabolic process / mitochondrial outer membrane / axon / synapse / dendrite / endoplasmic reticulum membrane / endoplasmic reticulum / mitochondrion
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1760 / 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. ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1760 / 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. / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Helix non-globular / Special
Similarity search - Domain/homology
Carnitine O-palmitoyltransferase 1, brain isoform
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsSamanta, S. / Situ, A.J. / Ulmer, T.S.
CitationJournal: Biopolymers / Year: 2014
Title: Structural characterization of the regulatory domain of brain carnitine palmitoyltransferase 1.
Authors: Samanta, S. / Situ, A.J. / Ulmer, T.S.
History
DepositionApr 18, 2013Deposition site: BMRB / Processing site: RCSB
Revision 1.0Sep 11, 2013Provider: repository / Type: Initial release
Revision 1.1Oct 2, 2013Group: Database references
Revision 1.2Feb 5, 2014Group: Database references
Revision 1.3Jun 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 1.4May 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, brain isoform


Theoretical massNumber of molelcules
Total (without water)5,7111
Polymers5,7111
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 / 40structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Carnitine O-palmitoyltransferase 1, brain isoform / CPT1-B / CPT IC / Carnitine O-palmitoyltransferase I / brain isoform / CPTI-B / Carnitine ...CPT1-B / CPT IC / Carnitine O-palmitoyltransferase I / brain isoform / CPTI-B / Carnitine palmitoyltransferase 1C


Mass: 5711.406 Da / Num. of mol.: 1 / Fragment: Regulatory Domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CPT1C, CATL1 / Plasmid: pET44-NCPT1C / Production host: Escherichia coli (E. coli) / References: UniProt: Q8TCG5

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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
141Quant J correlation

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Sample preparation

DetailsContents: 0.5 mM [U-100% 13C; U-100% 15N; U-80% 2H] protein, 150 mM dodecyltrimethylammonium chloride, 25 mM MES, 95% H2O/5% D2O
Solvent system: 95% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.5 mMentity-1[U-100% 13C; U-100% 15N; U-80% 2H]1
150 mMdodecyltrimethylammonium chloride-21
25 mMMES-31
Sample conditionsIonic strength: 0.175 / 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: 40 / Conformers submitted total number: 20

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