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- PDB-1a6x: STRUCTURE OF THE APO-BIOTIN CARBOXYL CARRIER PROTEIN (APO-BCCP87)... -

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Basic information

Entry
Database: PDB / ID: 1a6x
TitleSTRUCTURE OF THE APO-BIOTIN CARBOXYL CARRIER PROTEIN (APO-BCCP87) OF ESCHERICHIA COLI ACETYL-COA CARBOXYLASE, NMR, 49 STRUCTURES
ComponentsAPO-BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE
KeywordsCARRIER PROTEIN / ACETYL-COA CARBOXYLASE / BIOTIN CARBOXYL CARRIER PROTEIN / BACKBONE DYNAMICS
Function / homology
Function and homology information


acetyl-CoA carboxylase complex / malonyl-CoA biosynthetic process / acetyl-CoA carboxylase activity / fatty acid biosynthetic process / molecular adaptor activity / cytosol / cytoplasm
Similarity search - Function
Acetyl-CoA biotin carboxyl carrier / Biotin-binding site / Biotin-requiring enzymes attachment site. / RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain / Biotin-requiring enzyme / Biotinyl/lipoyl domain profile. / Biotin/lipoyl attachment / Single hybrid motif / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Biotin carboxyl carrier protein of acetyl-CoA carboxylase
Similarity search - Component
Biological speciesEscherichia coli BL21 (bacteria)
MethodSOLUTION NMR / distance geometry
AuthorsYao, X. / Wei, D. / Soden Junior, C. / Summers, M.F. / Beckett, D.
CitationJournal: Biochemistry / Year: 1997
Title: Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase.
Authors: Yao, X. / Wei, D. / Soden Jr., C. / Summers, M.F. / Beckett, D.
History
DepositionMar 4, 1998Processing site: BNL
Revision 1.0Oct 14, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4May 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: APO-BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE


Theoretical massNumber of molelcules
Total (without water)9,3421
Polymers9,3421
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)49 / 49LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein APO-BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE / APO-BCCP87


Mass: 9341.752 Da / Num. of mol.: 1 / Fragment: CARBOXYL-TERMINAL FRAGMENT, RESIDUES 70 - 156
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli BL21(DE3) (bacteria) / Species: Escherichia coli / Strain: BL21 (DE3) / Cell line: BL21 / Plasmid: PTM53 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P0ABD8, acetyl-CoA carboxylase

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY
131COSY
141HSQC
151NOESY-HSQC
161TOCSY-HSQC AND T1
171T2
181NOE MEASUREMENTS

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Sample preparation

DetailsContents: PHOSPHATE BUFFER
Sample conditionspH: 7.5 / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: GE GE OMEGA PSG / Manufacturer: GE / Model: GE OMEGA PSG / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
DIANAGUNTERT,WUTHRICHrefinement
DIANAstructure solution
RefinementMethod: distance geometry / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE.
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 49 / Conformers submitted total number: 49

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