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- PDB-4k84: Crystal structure of human ceramide-1-phosphate transfer protein ... -

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Basic information

Entry
Database: PDB / ID: 4k84
TitleCrystal structure of human ceramide-1-phosphate transfer protein (CPTP) in complex with 16:0 ceramide-1-phosphate (16:0-C1P)
ComponentsGlycolipid transfer protein domain-containing protein 1
KeywordsLIPID TRANSPORT / Lipid transfer protein / GLTP-fold / CPTP / C1P / Ceramide-1-phosphate / Protein-lipid complex / Eicosanoid
Function / homology
Function and homology information


ceramide 1-phosphate transport / ceramide transport / ceramide 1-phosphate binding / ceramide 1-phosphate transfer activity / Glycosphingolipid transport / intermembrane lipid transfer / negative regulation of NLRP3 inflammasome complex assembly / nuclear outer membrane / negative regulation of interleukin-1 beta production / negative regulation of autophagy ...ceramide 1-phosphate transport / ceramide transport / ceramide 1-phosphate binding / ceramide 1-phosphate transfer activity / Glycosphingolipid transport / intermembrane lipid transfer / negative regulation of NLRP3 inflammasome complex assembly / nuclear outer membrane / negative regulation of interleukin-1 beta production / negative regulation of autophagy / phospholipid binding / endosome membrane / Golgi apparatus / plasma membrane / cytosol
Similarity search - Function
Glycolipid transfer protein domain / Glycolipid transfer protein superfamily / Glycolipid transfer protein (GLTP) / Glycolipid transfer protein, GLTP / Glycolipid transfer protein / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Chem-1PX / Ceramide-1-phosphate transfer protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.897 Å
AuthorsSimanshu, D.K. / Brown, R.E. / Patel, D.J.
CitationJournal: Nature / Year: 2013
Title: Non-vesicular trafficking by a ceramide-1-phosphate transfer protein regulates eicosanoids.
Authors: Simanshu, D.K. / Kamlekar, R.K. / Wijesinghe, D.S. / Zou, X. / Zhai, X. / Mishra, S.K. / Molotkovsky, J.G. / Malinina, L. / Hinchcliffe, E.H. / Chalfant, C.E. / Brown, R.E. / Patel, D.J.
History
DepositionApr 17, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 17, 2013Provider: repository / Type: Initial release
Revision 1.1Sep 11, 2013Group: Database references
Revision 1.2Nov 15, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.3Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Apr 3, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Glycolipid transfer protein domain-containing protein 1
B: Glycolipid transfer protein domain-containing protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)50,2044
Polymers48,9682
Non-polymers1,2362
Water7,909439
1
A: Glycolipid transfer protein domain-containing protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,1022
Polymers24,4841
Non-polymers6181
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Glycolipid transfer protein domain-containing protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,1022
Polymers24,4841
Non-polymers6181
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)62.604, 50.291, 62.870
Angle α, β, γ (deg.)90.00, 100.11, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Glycolipid transfer protein domain-containing protein 1


Mass: 24484.154 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GLTPD1 / Plasmid: pET-SUMO / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) Star / References: UniProt: Q5TA50
#2: Chemical ChemComp-1PX / (2S,3R,4E)-2-(hexadecanoylamino)-3-hydroxyoctadec-4-en-1-yl dihydrogen phosphate


Mass: 617.881 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H68NO6P
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 439 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 1.99 Å3/Da / Density % sol: 38.18 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5
Details: 0.1 M MMT buffer pH 5.0, 25% PEG1500, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 1.2398 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Aug 8, 2009
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.2398 Å / Relative weight: 1
ReflectionResolution: 1.9→50 Å / Num. obs: 30620 / % possible obs: 99.7 % / Redundancy: 6.8 % / Rmerge(I) obs: 0.079 / Net I/σ(I): 10
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsDiffraction-ID% possible all
1.9-1.974.50.269196.8
1.97-2.0560.2261100
2.05-2.146.90.1841100
2.14-2.257.10.1651100
2.25-2.397.30.1241100
2.39-2.587.30.1051100
2.58-2.847.30.0891100
2.84-3.257.30.0761100
3.25-4.097.10.0621100
4.09-5070.047199.7

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
PHENIX1.5_2refinement
PDB_EXTRACT3.11data extraction
ADSCQuantumdata collection
HKL-2000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: Human ceramide-1-phosphate transfer protein in complex with C2 Ceramide-1-phosphate (2:0 C1P)

Resolution: 1.897→40.278 Å / Occupancy max: 1 / Occupancy min: 0.36 / SU ML: 0.2 / σ(F): 0.11 / Phase error: 22.43 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2133 1515 5.06 %
Rwork0.1622 --
obs0.1647 29952 97.38 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 43.821 Å2 / ksol: 0.36 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--0.7468 Å2-0 Å2-0.9344 Å2
2---1.8039 Å20 Å2
3---2.5507 Å2
Refinement stepCycle: LAST / Resolution: 1.897→40.278 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3297 0 84 439 3820
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0073501
X-RAY DIFFRACTIONf_angle_d0.9364739
X-RAY DIFFRACTIONf_dihedral_angle_d18.0081359
X-RAY DIFFRACTIONf_chiral_restr0.06527
X-RAY DIFFRACTIONf_plane_restr0.005599
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8968-1.9580.25911030.16622363X-RAY DIFFRACTION89
1.958-2.0280.2351390.16972517X-RAY DIFFRACTION95
2.028-2.10920.22421310.16292567X-RAY DIFFRACTION96
2.1092-2.20520.20791490.15382495X-RAY DIFFRACTION97
2.2052-2.32140.19971380.15272599X-RAY DIFFRACTION98
2.3214-2.46690.2221300.15692613X-RAY DIFFRACTION99
2.4669-2.65730.2251400.16032618X-RAY DIFFRACTION99
2.6573-2.92460.21931440.16612614X-RAY DIFFRACTION99
2.9246-3.34770.21371430.16442678X-RAY DIFFRACTION100
3.3477-4.2170.1951550.14562676X-RAY DIFFRACTION100
4.217-40.28710.20111430.17242697X-RAY DIFFRACTION99

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