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- PDB-1gzp: CD1b in complex with GM2 ganglioside -

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Basic information

Entry
Database: PDB / ID: 1gzp
TitleCD1b in complex with GM2 ganglioside
Components
  • B2-MICROGLOBULIN
  • T-CELL SURFACE GLYCOPROTEIN CD1B
KeywordsGLYCOPROTEIN / LIPID / GANGLIOSIDE / MHC / ANTIGEN PRESENTATION
Function / homology
Function and homology information


: / : / endogenous lipid antigen binding / exogenous lipid antigen binding / antigen processing and presentation, endogenous lipid antigen via MHC class Ib / antigen processing and presentation, exogenous lipid antigen via MHC class Ib / lipopeptide binding / retina homeostasis / regulation of membrane depolarization / positive regulation of ferrous iron binding ...: / : / endogenous lipid antigen binding / exogenous lipid antigen binding / antigen processing and presentation, endogenous lipid antigen via MHC class Ib / antigen processing and presentation, exogenous lipid antigen via MHC class Ib / lipopeptide binding / retina homeostasis / regulation of membrane depolarization / positive regulation of ferrous iron binding / positive regulation of transferrin receptor binding / early endosome lumen / positive regulation of receptor binding / Nef mediated downregulation of MHC class I complex cell surface expression / DAP12 interactions / negative regulation of receptor binding / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / cellular response to iron(III) ion / negative regulation of forebrain neuron differentiation / ER to Golgi transport vesicle membrane / response to molecule of bacterial origin / regulation of erythrocyte differentiation / regulation of iron ion transport / MHC class I peptide loading complex / HFE-transferrin receptor complex / T cell mediated cytotoxicity / cellular response to iron ion / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / MHC class I protein complex / multicellular organismal-level iron ion homeostasis / positive regulation of T cell mediated cytotoxicity / peptide antigen assembly with MHC class II protein complex / negative regulation of neurogenesis / positive regulation of receptor-mediated endocytosis / MHC class II protein complex / cellular response to nicotine / recycling endosome membrane / specific granule lumen / phagocytic vesicle membrane / peptide antigen binding / positive regulation of cellular senescence / antigen processing and presentation of exogenous peptide antigen via MHC class II / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / Interferon gamma signaling / positive regulation of immune response / negative regulation of epithelial cell proliferation / Modulation by Mtb of host immune system / positive regulation of T cell activation / antimicrobial humoral immune response mediated by antimicrobial peptide / sensory perception of smell / negative regulation of neuron projection development / tertiary granule lumen / DAP12 signaling / MHC class II protein complex binding / late endosome membrane / T cell differentiation in thymus / positive regulation of protein binding / ER-Phagosome pathway / antibacterial humoral response / iron ion transport / protein refolding / early endosome membrane / protein homotetramerization / cellular response to lipopolysaccharide / intracellular iron ion homeostasis / defense response to Gram-negative bacterium / amyloid fibril formation / adaptive immune response / learning or memory / endosome membrane / defense response to Gram-positive bacterium / immune response / Amyloid fiber formation / lysosomal membrane / endoplasmic reticulum lumen / external side of plasma membrane / Golgi membrane / focal adhesion / innate immune response / intracellular membrane-bounded organelle / Neutrophil degranulation / SARS-CoV-2 activates/modulates innate and adaptive immune responses / Golgi apparatus / cell surface / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / membrane / identical protein binding / plasma membrane / cytosol
Similarity search - Function
MHC-I family domain / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / Beta-2-Microglobulin / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type ...MHC-I family domain / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / Beta-2-Microglobulin / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
DODECANE / Chem-GM2 / DOCOSANE / Beta-2-microglobulin / T-cell surface glycoprotein CD1b / Beta-2-microglobulin
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsGadola, S.D. / Zaccai, N.R. / Harlos, K. / Shepherd, D. / Ritter, G. / Schmidt, R.R. / Jones, E.Y. / Cerundolo, V.
CitationJournal: Nat. Immunol. / Year: 2002
Title: Structure of human CD1b with bound ligands at 2.3 A, a maze for alkyl chains.
Authors: Gadola, S.D. / Zaccai, N.R. / Harlos, K. / Shepherd, D. / Castro-Palomino, J.C. / Ritter, G. / Schmidt, R.R. / Jones, E.Y. / Cerundolo, V.
History
DepositionMay 24, 2002Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 31, 2002Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 28, 2018Group: Database references / Source and taxonomy / Category: citation / entity_src_gen
Item: _citation.journal_abbrev / _citation.page_last ..._citation.journal_abbrev / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_scientific_name / _entity_src_gen.pdbx_host_org_strain / _entity_src_gen.pdbx_host_org_vector
Revision 1.4May 22, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.temp
Revision 1.5Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: T-CELL SURFACE GLYCOPROTEIN CD1B
B: B2-MICROGLOBULIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,1935
Polymers44,9682
Non-polymers1,2253
Water72140
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)87.527, 176.885, 75.250
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

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Protein , 2 types, 2 molecules AB

#1: Protein T-CELL SURFACE GLYCOPROTEIN CD1B / CD1B ANTIGEN


Mass: 33088.215 Da / Num. of mol.: 1 / Fragment: RESIDUES 18-295
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET23D / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: P29016
#2: Protein B2-MICROGLOBULIN


Mass: 11879.356 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET23D / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: P01884, UniProt: P61769*PLUS

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Non-polymers , 4 types, 43 molecules

#3: Chemical ChemComp-GM2 / N-[(1S,2S)-2-HYDROXY-1-({[(2R,3R,4S,5S,6R)-3,4,5-TRIHYDROXY-6-(HYDROXYMETHYL)TETRAHYDRO-2H-PYRAN-2-YL]OXY}METHYL)OCTADECYL]OCTADECANAMIDE


Mass: 744.137 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C43H85NO8
#4: Chemical ChemComp-D12 / DODECANE / Dodecane


Mass: 170.335 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C12H26
#5: Chemical ChemComp-TWT / DOCOSANE / Higher alkanes


Mass: 310.601 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C22H46
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 40 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsRESIDUES GLYCINE A278 AND PROLINE A279 ARE THE STARTING RESIDUES OF A BIRA TAG ...RESIDUES GLYCINE A278 AND PROLINE A279 ARE THE STARTING RESIDUES OF A BIRA TAG (GPGSGGGLNDIFEAQKIEWH) WHICH WAS LOCATED AT THE C-TERMINUS OF THE RECOMBINANT CD1B HEAVY CHAIN.

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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: 3.24 Å3/Da / Density % sol: 64 %
Crystal growTemperature: 293 K / pH: 7.1
Details: 20 DEGREE C 2UL OF PROTEIN + 1UL OF MOTHER LIQUOR 0.2M LITHIUM NITRATE 20% W/V POLYETHYLENE GLYCOL 3350, PH 7.1
Crystal grow
*PLUS
Temperature: 20 ℃ / Method: vapor diffusion, sitting drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
10.2 Mlithium nitrate1reservoir
220 %(w/v)PEG33501reservoirpH7.1
35 mg/mlprotein1drop

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.93
DetectorType: ADSC CCD / Detector: CCD / Date: Oct 15, 2001
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.93 Å / Relative weight: 1
ReflectionResolution: 2.8→100 Å / Num. obs: 89500 / % possible obs: 87.4 % / Observed criterion σ(I): -0.5 / Redundancy: 6.8 % / Biso Wilson estimate: 95.2 Å2 / Rmerge(I) obs: 0.103 / Net I/σ(I): 13.7
Reflection shellResolution: 2.8→2.9 Å / Rmerge(I) obs: 0.325 / Mean I/σ(I) obs: 1.8 / % possible all: 71.1
Reflection
*PLUS
Lowest resolution: 100 Å / Num. obs: 13203 / % possible obs: 88.8 % / Num. measured all: 89500
Reflection shell
*PLUS
Highest resolution: 2.8 Å / Lowest resolution: 2.91 Å / % possible obs: 71.1 %

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Processing

Software
NameVersionClassification
CNS1.1refinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1CD1

1cd1


Resolution: 2.8→34.78 Å / Rfactor Rfree error: 0.012 / Data cutoff high absF: 355814.88 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
RfactorNum. reflection% reflectionSelection details
Rfree0.273 535 4.1 %RANDOM
Rwork0.225 ---
obs0.225 12918 87.4 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 14.0445 Å2 / ksol: 0.282575 e/Å3
Displacement parametersBiso mean: 50.2 Å2
Baniso -1Baniso -2Baniso -3
1-2.43 Å20 Å20 Å2
2---6.93 Å20 Å2
3---4.5 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.48 Å0.37 Å
Luzzati d res low-5 Å
Luzzati sigma a0.7 Å0.44 Å
Refinement stepCycle: LAST / Resolution: 2.8→34.78 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2992 0 86 40 3118
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.012
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.6
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d26.5
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d1.46
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it2.351.5
X-RAY DIFFRACTIONc_mcangle_it3.92
X-RAY DIFFRACTIONc_scbond_it4.012
X-RAY DIFFRACTIONc_scangle_it5.722.5
LS refinement shellResolution: 2.8→2.98 Å / Rfactor Rfree error: 0.051 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.428 70 4.3 %
Rwork0.367 1543 -
obs--67.2 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2WATER_REP.PARAMWATER.TOP
X-RAY DIFFRACTION3GM2_11.PARAMGM2_11.TOP
Refinement
*PLUS
Lowest resolution: 100 Å / Rfactor Rfree: 0.274 / Rfactor Rwork: 0.223
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_angle_deg1.62
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg26.5
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg1.46
LS refinement shell
*PLUS
Lowest resolution: 2.91 Å

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