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- PDB-4asv: Solution structure of the N-terminal dimerisation domain of Sgt2 -

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Basic information

Entry
Database: PDB / ID: 4asv
TitleSolution structure of the N-terminal dimerisation domain of Sgt2
ComponentsSMALL GLUTAMINE-RICH TETRATRICOPEPTIDE REPEAT-CONTAINING PROTEIN 2
KeywordsCHAPERONE / MEMBRANE / TAIL-ANCHORED / POST-TRANSLATIONAL TARGETING
Function / homology
Function and homology information


TRC complex / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / post-translational protein targeting to endoplasmic reticulum membrane / response to heat / molecular adaptor activity / membrane / identical protein binding / cytosol / cytoplasm
Similarity search - Function
SGTA, homodimerisation domain / Homodimerisation domain of SGTA / : / Immunoglobulin FC, subunit C / Tetratricopeptide repeat 1 / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat ...SGTA, homodimerisation domain / Homodimerisation domain of SGTA / : / Immunoglobulin FC, subunit C / Tetratricopeptide repeat 1 / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Tetratricopeptide-like helical domain superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Small glutamine-rich tetratricopeptide repeat-containing protein 2
Similarity search - Component
Biological speciesSACCHAROMYCES CEREVISIAE (brewer's yeast)
MethodSOLUTION NMR / ARIA
AuthorsSimon, A.C. / Simpson, P.J. / Goldstone, R.M. / Krysztofinska, E.M. / Murray, J.W. / High, S. / Isaacson, R.L.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2013
Title: Structure of the Sgt2/Get5 Complex Provides Insights Into Get-Mediated Targeting of Tail-Anchored Membrane Proteins
Authors: Simon, A.C. / Simpson, P.J. / Goldstone, R.M. / Krysztofinska, E.M. / Murray, J.W. / High, S. / Isaacson, R.L.
History
DepositionMay 3, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 16, 2013Provider: repository / Type: Initial release
Revision 1.1Jan 30, 2013Group: Database references
Revision 1.2Mar 6, 2013Group: Database references
Revision 2.0Jun 14, 2023Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Other
Category: atom_site / database_2 ...atom_site / database_2 / pdbx_database_status / pdbx_nmr_spectrometer
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_spectrometer.model

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Structure visualization

Structure viewerMolecule:
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Assembly

Deposited unit
A: SMALL GLUTAMINE-RICH TETRATRICOPEPTIDE REPEAT-CONTAINING PROTEIN 2
B: SMALL GLUTAMINE-RICH TETRATRICOPEPTIDE REPEAT-CONTAINING PROTEIN 2


Theoretical massNumber of molelcules
Total (without water)20,1962
Polymers20,1962
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100LOWEST ENERGY
RepresentativeModel #1

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Components

#1: Protein SMALL GLUTAMINE-RICH TETRATRICOPEPTIDE REPEAT-CONTAINING PROTEIN 2 / SGT2_NT / SGT/UBP / VIRAL PROTEIN U-BINDING PROTEIN


Mass: 10098.163 Da / Num. of mol.: 2 / Fragment: DIMERISATION DOMAIN, RESIDUES 1-78
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast)
Description: GENOMIC DNA / Plasmid: PET46-SGT2_NT / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA / References: UniProt: Q12118

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR detailsText: NONE

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Sample preparation

DetailsContents: 10% WATER/90% D2O
Sample conditionsIonic strength: 250 mM / pH: 6.0 / Pressure: 1 atm / Temperature: 308.0 K

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NMR measurement

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

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Processing

NMR softwareName: ARIA / Developer: BARDIAUX B,MALLIAVIN T,NILGES M / Classification: refinement
RefinementMethod: ARIA / Software ordinal: 1 / Details: BMRB 18341
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 20

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