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- PDB-1jjj: SOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID... -

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Entry
Database: PDB / ID: 1jjj
TitleSOLUTION STRUCTURE OF RECOMBINANT HUMAN EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN
ComponentsEPIDERMAL-TYPE FATTY ACID BINDING PROTEIN (E-FABP)
KeywordsLIPID BINDING PROTEIN / BETA BARREL / FATTY ACID CARRIER / HOLO FORM / NMR SPECTROSCOPY / 15N ISOTOPE ENRICHMENT
Function / homology
Function and homology information


regulation of prostaglandin biosynthetic process / regulation of retrograde trans-synaptic signaling by endocanabinoid / lipid transport across blood-brain barrier / retrograde trans-synaptic signaling by endocannabinoid / positive regulation of peroxisome proliferator activated receptor signaling pathway / negative regulation of D-glucose transmembrane transport / regulation of sensory perception of pain / phosphatidylcholine biosynthetic process / retinoic acid binding / Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin ...regulation of prostaglandin biosynthetic process / regulation of retrograde trans-synaptic signaling by endocanabinoid / lipid transport across blood-brain barrier / retrograde trans-synaptic signaling by endocannabinoid / positive regulation of peroxisome proliferator activated receptor signaling pathway / negative regulation of D-glucose transmembrane transport / regulation of sensory perception of pain / phosphatidylcholine biosynthetic process / retinoic acid binding / Differentiation of Keratinocytes in Interfollicular Epidermis in Mammalian Skin / Signaling by Retinoic Acid / long-chain fatty acid transmembrane transporter activity / Triglyceride catabolism / epidermis development / postsynaptic cytosol / long-chain fatty acid transport / fatty acid transport / postsynaptic density, intracellular component / secretory granule membrane / fatty acid binding / lipid metabolic process / glucose metabolic process / azurophil granule lumen / glucose homeostasis / positive regulation of cold-induced thermogenesis / postsynaptic density / synapse / lipid binding / Neutrophil degranulation / glutamatergic synapse / extracellular exosome / extracellular region / nucleoplasm / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Cytosolic fatty-acid binding proteins signature. / Intracellular lipid binding protein / Cytosolic fatty-acid binding / Lipocalin / cytosolic fatty-acid binding protein family / Lipocalin/cytosolic fatty-acid binding domain / Calycin beta-barrel core domain / Calycin / Lipocalin / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Fatty acid-binding protein 5
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, ENERGY MINIMIZATION
AuthorsGutierrez-Gonzalez, L.H. / Ludwig, C. / Hohoff, C. / Rademacher, M. / Hanhoff, T. / Rueterjans, H. / Spener, F. / Luecke, C.
Citation
Journal: BIOCHEM.J. / Year: 2002
Title: Solution structure and backbone dynamics of human epidermal-type fatty acid-binding protein (E-FABP)
Authors: Gutierrez-Gonzalez, L.H. / Ludwig, C. / Hohoff, C. / Rademacher, M. / Hanhoff, T. / Rueterjans, H. / Spener, F. / Luecke, C.
#1: Journal: Biochemistry / Year: 1999
Title: Expression, Purification, and Crystal Structure Determination of Recombinant Human Epidermal-Type Fatty Acid Binding Protein
Authors: Hohoff, C. / Boerchers, T. / Ruestow, B. / Spener, F. / Van Tilbeurgh, H.
History
DepositionJul 6, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 19, 2002Provider: repository / Type: Initial release
Revision 1.1Oct 21, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4Nov 6, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN (E-FABP)


Theoretical massNumber of molelcules
Total (without water)15,1851
Polymers15,1851
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 / 300target function
Representative

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Components

#1: Protein EPIDERMAL-TYPE FATTY ACID BINDING PROTEIN (E-FABP)


Mass: 15185.457 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FABP5 / Plasmid: PET3D / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q01469
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D TOCSY
1212D NOESY
1312D 15N-HSQC
1412D 15N-HTQC
1513D 15N-TOCSY-HSQC
1613D 15N-NOESY-HSQC

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Sample preparation

DetailsContents: 1.5-2 MM E-FABP PHOSPHATE BUFFER; 0.05% SODIUM AZIDE
Sample conditionsIonic strength: 20 mM POTASSIUM PHOSPHATE / pH: 5.6 / Pressure: AMBIENT / Temperature: 298.00 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
Discover97MSIrefinement
XwinNMR1.3structure solution
AURELIA2.5.9structure solution
DYANA1.5structure solution
RefinementMethod: TORSION ANGLE DYNAMICS, SIMULATED ANNEALING, ENERGY MINIMIZATION
Software ordinal: 1
Details: THE STRUCTURES ARE BASED ON A TOTAL OF 2008 NOE-DERIVED DISTANCE RESTRAINTS
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 300 / Conformers submitted total number: 20

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