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- PDB-3egx: Crystal structure of the mammalian COPII-coat protein Sec23a/24a ... -

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Basic information

Entry
Database: PDB / ID: 3egx
TitleCrystal structure of the mammalian COPII-coat protein Sec23a/24a complexed with the SNARE protein Sec22b and bound to the transport signal sequence of the SNARE protein Bet1
Components
  • 9-residue synthetic peptide from SNARE protein Bet1
  • Protein transport protein Sec23AProtein targeting
  • Protein transport protein Sec24AProtein targeting
  • Vesicle-trafficking protein SEC22b
KeywordsPROTEIN TRANSPORT / COPII coat protein / vesicle transport / transport signal sequence / Disease mutation / Endoplasmic reticulum / ER-Golgi transport / Golgi apparatus / Membrane / Transport / Phosphoprotein / Transmembrane
Function / homology
Function and homology information


vesicle fusion with Golgi apparatus / Golgi trans cisterna / regulation of cholesterol transport / COPII vesicle coating / COPII-coated vesicle cargo loading / integral component of Golgi membrane / COPII vesicle coat / negative regulation of autophagosome assembly / SNARE complex / SNAP receptor activity ...vesicle fusion with Golgi apparatus / Golgi trans cisterna / regulation of cholesterol transport / COPII vesicle coating / COPII-coated vesicle cargo loading / integral component of Golgi membrane / COPII vesicle coat / negative regulation of autophagosome assembly / SNARE complex / SNAP receptor activity / Regulation of cholesterol biosynthesis by SREBP (SREBF) / Cargo concentration in the ER / retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum / COPII-mediated vesicle transport / COPI-dependent Golgi-to-ER retrograde traffic / endoplasmic reticulum to Golgi vesicle-mediated transport / COPI-mediated anterograde transport / extrinsic component of membrane / endoplasmic reticulum exit site / SNARE binding / endoplasmic reticulum-Golgi intermediate compartment membrane / MHC class II antigen presentation / transport vesicle / GTPase activator activity / cholesterol homeostasis / protein localization to plasma membrane / intracellular protein transport / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / positive regulation of protein secretion / positive regulation of protein catabolic process / ER to Golgi transport vesicle membrane / melanosome / phagocytic vesicle membrane / protein transport / ER-Phagosome pathway / endoplasmic reticulum-Golgi intermediate compartment / Golgi membrane / endoplasmic reticulum membrane / perinuclear region of cytoplasm / zinc ion binding / membrane / integral component of membrane / cytosol
Similarity search - Function
BET1-like protein / BET1, SNARE domain / Vesicle-trafficking protein Sec22 / Longin domain / Longin domain profile. / Regulated-SNARE-like domain / Regulated-SNARE-like domain / Longin domain / beta-sandwich domain of Sec23/24 / Sec23/Sec24 helical domain ...BET1-like protein / BET1, SNARE domain / Vesicle-trafficking protein Sec22 / Longin domain / Longin domain profile. / Regulated-SNARE-like domain / Regulated-SNARE-like domain / Longin domain / beta-sandwich domain of Sec23/24 / Sec23/Sec24 helical domain / Protein transport protein Sec23 / Sec23, C-terminal / Sec24-like, trunk domain / Sec23/Sec24 beta-sandwich / Sec23/Sec24, trunk domain / Zinc finger, Sec23/Sec24-type / Sec23/Sec24, helical domain / Sec23/Sec24 zinc finger / Sec23/Sec24 helical domain / Sec23/Sec24 trunk domain / Sec23/Sec24 beta-sandwich domain / Sec23/Sec24 helical domain superfamily / Zn-finger domain of Sec23/24 / Zinc finger, Sec23/Sec24-type superfamily / Synaptobrevin / Synaptobrevin / Gelsolin-like domain superfamily / v-SNARE, coiled-coil homology domain / v-SNARE coiled-coil homology domain profile. / Helical region found in SNAREs / t-SNARE coiled-coil homology domain profile. / Target SNARE coiled-coil homology domain / Gelsolin-like domain / Gelsolin repeat / Severin / Severin / Longin-like domain superfamily / ADF-H/Gelsolin-like domain superfamily / von Willebrand factor, type A domain / von Willebrand factor A-like domain superfamily / Beta-Lactamase / Four Helix Bundle (Hemerythrin (Met), subunit A) / SH3 type barrels. / Roll / Up-down Bundle / Immunoglobulin-like / Sandwich / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
BET1 homolog / Vesicle-trafficking protein SEC22b / Protein transport protein Sec24A / Protein transport protein Sec23A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 3.3 Å
AuthorsGoldberg, J. / Mancias, J.D.
CitationJournal: Embo J. / Year: 2008
Title: Structural basis of cargo membrane protein discrimination by the human COPII coat machinery.
Authors: Mancias, J.D. / Goldberg, J.
History
DepositionSep 11, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 21, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Protein transport protein Sec23A
B: Protein transport protein Sec24A
C: Vesicle-trafficking protein SEC22b
D: 9-residue synthetic peptide from SNARE protein Bet1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)189,6796
Polymers189,5484
Non-polymers1312
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4880 Å2
ΔGint-20 kcal/mol
Surface area66210 Å2
MethodPISA
Unit cell
Length a, b, c (Å)148.150, 97.230, 129.510
Angle α, β, γ (deg.)90.00, 90.01, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Protein transport protein Sec23A / Protein targeting / SEC23-related protein A


Mass: 86178.414 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SEC23A / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q15436
#2: Protein Protein transport protein Sec24A / Protein targeting / SEC24-related protein A


Mass: 84336.820 Da / Num. of mol.: 1 / Fragment: Conserved core, UNP residues 346-1093
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SEC24A / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: O95486
#3: Protein Vesicle-trafficking protein SEC22b / SEC22 vesicle-trafficking protein homolog B / SEC22 vesicle-trafficking protein-like 1 / ERS24 / ERS-24


Mass: 18031.645 Da / Num. of mol.: 1 / Fragment: cytoplasmic domainn, UNP residues 1-157
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SEC22B, SEC22L1 / Production host: Escherichia coli (E. coli) / References: UniProt: O75396
#4: Protein/peptide 9-residue synthetic peptide from SNARE protein Bet1


Mass: 1000.984 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: synthetic 9-residue peptide / References: UniProt: O15155*PLUS
#5: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

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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: 2.46 Å3/Da / Density % sol: 50.01 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.9
Details: 10% (w/v) PEG 4000, 0.1 M NaCl, 0.5 M sodium acetate, 50 mM Tris buffer, pH 7.9, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 200 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: May 5, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.3→25 Å / Num. obs: 24079 / % possible obs: 92 % / Observed criterion σ(F): 1 / Redundancy: 2.7 % / Rmerge(I) obs: 0.111 / Net I/σ(I): 9.6
Reflection shellResolution: 3.3→3.4 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.394 / Mean I/σ(I) obs: 2.2 / % possible all: 95.1

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling
CNSphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 3.3→25 Å / Cross valid method: THROUGHOUT / σ(F): 1 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.292 1204 random
Rwork0.206 --
obs-24079 -
Refinement stepCycle: LAST / Resolution: 3.3→25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12521 0 2 0 12523

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