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- PDB-2j3w: The crystal structure of the bet3-trs31-sedlin complex. -

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Basic information

Entry
Database: PDB / ID: 2j3w
TitleThe crystal structure of the bet3-trs31-sedlin complex.
Components
  • TRAFFICKING PROTEIN PARTICLE COMPLEX PROTEIN 2
  • TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 3
  • ZGC 92866
KeywordsTRANSPORT / MULTISUBUNIT TETHERING FACTOR / TRAPP / PALMITATE / LIPOPROTEIN / ER-GOLGI TRANSPORT / ENDOPLASMIC RETICULUM / TRANSCRIPTION / GOLGI APPARATUS / VESICLE TRANSPORT
Function / homology
Function and homology information


COPII-mediated vesicle transport / RAB GEFs exchange GTP for GDP on RABs / vesicle coating / vesicle tethering / RAB GEFs exchange GTP for GDP on RABs / TRAPPI protein complex / COPII-mediated vesicle transport / TRAPPII protein complex / TRAPPIII protein complex / TRAPP complex ...COPII-mediated vesicle transport / RAB GEFs exchange GTP for GDP on RABs / vesicle coating / vesicle tethering / RAB GEFs exchange GTP for GDP on RABs / TRAPPI protein complex / COPII-mediated vesicle transport / TRAPPII protein complex / TRAPPIII protein complex / TRAPP complex / COPII vesicle coating / intra-Golgi vesicle-mediated transport / cis-Golgi network membrane / endoplasmic reticulum-Golgi intermediate compartment / endoplasmic reticulum to Golgi vesicle-mediated transport / transcription corepressor binding / skeletal system development / transmembrane transporter binding / Golgi membrane / intracellular membrane-bounded organelle / positive regulation of gene expression / perinuclear region of cytoplasm / Golgi apparatus / endoplasmic reticulum / nucleoplasm / nucleus / cytosol / cytoplasm
Similarity search - Function
Beta-Lactamase - #70 / Trafficking protein particle complex subunit 3 / Trafficking protein particle complex subunit 2 / Sedlin, N-terminal conserved region / TRAPP I complex, subunit 5 / Bet3 family / Transport protein particle (TRAPP) component / Transport protein particle (TRAPP) component / Muramoyl-pentapeptide Carboxypeptidase; domain 2 / NO signalling/Golgi transport ligand-binding domain superfamily ...Beta-Lactamase - #70 / Trafficking protein particle complex subunit 3 / Trafficking protein particle complex subunit 2 / Sedlin, N-terminal conserved region / TRAPP I complex, subunit 5 / Bet3 family / Transport protein particle (TRAPP) component / Transport protein particle (TRAPP) component / Muramoyl-pentapeptide Carboxypeptidase; domain 2 / NO signalling/Golgi transport ligand-binding domain superfamily / Longin-like domain superfamily / Beta-Lactamase / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
PALMITIC ACID / Trafficking protein particle complex subunit 3 / Trafficking protein particle complex subunit 5 / Trafficking protein particle complex subunit 2
Similarity search - Component
Biological speciesMUS MUSCULUS (house mouse)
BRACHYDANIO RERIO (zebrafish)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsKim, Y.-G. / Oh, B.-H.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2006
Title: The Architecture of the Multisubunit Trapp I Complex Suggests a Model for Vesicle Tethering.
Authors: Kim, Y.-G. / Raunser, S. / Munger, C. / Wagner, J. / Song, Y.-L. / Cygler, M. / Walz, T. / Oh, B.-H. / Sacher, M.
History
DepositionAug 23, 2006Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 27, 2006Provider: repository / Type: Initial release
Revision 1.1Oct 26, 2011Group: Atomic model / Database references ...Atomic model / Database references / Derived calculations / Non-polymer description / Other / Refinement description / Structure summary / Version format compliance
Revision 1.2Aug 7, 2013Group: Other / Source and taxonomy

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TRAFFICKING PROTEIN PARTICLE COMPLEX PROTEIN 2
B: ZGC 92866
C: TRAFFICKING PROTEIN PARTICLE COMPLEX PROTEIN 2
D: TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 3
E: TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 3
F: ZGC 92866
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,9468
Polymers116,4336
Non-polymers5132
Water3,873215
1
C: TRAFFICKING PROTEIN PARTICLE COMPLEX PROTEIN 2
D: TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 3
F: ZGC 92866
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,4734
Polymers58,2173
Non-polymers2561
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5090 Å2
ΔGint-41.5 kcal/mol
Surface area21370 Å2
MethodPISA
2
A: TRAFFICKING PROTEIN PARTICLE COMPLEX PROTEIN 2
B: ZGC 92866
E: TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,4734
Polymers58,2173
Non-polymers2561
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5210 Å2
ΔGint-38.7 kcal/mol
Surface area21850 Å2
MethodPISA
Unit cell
Length a, b, c (Å)232.211, 63.063, 72.018
Angle α, β, γ (deg.)90.00, 91.72, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein TRAFFICKING PROTEIN PARTICLE COMPLEX PROTEIN 2 / SEDLIN


Mass: 16705.027 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PPROEXHTA, PET15B, PET30A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9CQP2
#2: Protein ZGC 92866


Mass: 21059.367 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) BRACHYDANIO RERIO (zebrafish) / Plasmid: PPROEXHTA, PET15B, PET30A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q6DGL5
#3: Protein TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 3 / BET3 HOMOLOG


Mass: 20452.227 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PPROEXHTA, PET15B, PET30A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O55013
#4: Chemical ChemComp-PLM / PALMITIC ACID / Palmitic acid


Mass: 256.424 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C16H32O2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 215 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.3 Å3/Da / Density % sol: 47 %
Crystal growpH: 8
Details: 20% (W/V) PEG3350, 0.2 M MGCL2, 2% (W/V) BENZAMIDINE AND 0.1 M TRIS HCL (PH 8.0)

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Data collection

DiffractionMean temperature: 103 K
Diffraction sourceSource: SYNCHROTRON / Site: PAL/PLS / Beamline: 4A / Wavelength: 1
DetectorType: ADSC CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.1→30 Å / Num. obs: 57111 / % possible obs: 93 % / Observed criterion σ(I): 0 / Redundancy: 5.1 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 29
Reflection shellHighest resolution: 2.1 Å / Mean I/σ(I) obs: 4.2 / % possible all: 73.4

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Processing

Software
NameClassification
CNSrefinement
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→30 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 1
RfactorNum. reflection% reflectionSelection details
Rfree0.2765 2892 4.7 %RANDOM
Rwork0.2296 ---
obs0.2296 57111 93.6 %-
Solvent computationBsol: 39.3699 Å2 / ksol: 0.347067 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-5.27 Å20 Å211.263 Å2
2--7.183 Å20 Å2
3----12.454 Å2
Refinement stepCycle: LAST / Resolution: 2.1→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7348 0 34 215 7597
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.0073
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_deg1.1519
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_scangle_it
Xplor file
Refine-IDSerial noParam file
X-RAY DIFFRACTION1PROTEIN_REP.PARAM
X-RAY DIFFRACTION2PLM.PAR
X-RAY DIFFRACTION3WATER_REP.PARAM

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