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- SASDB45: Trimeric periplasmic holdase chaperone protein Skp -

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Basic information

Entry
Database: SASBDB / ID: SASDB45
SampleTrimeric periplasmic holdase chaperone protein Skp
  • Periplasmic holdase chaperone protein Skp (protein), Skp, Escherichia coli
Function / homology
Function and homology information


protein insertion into membrane from inner side / Gram-negative-bacterium-type cell outer membrane assembly / protein maturation by protein folding / chaperone-mediated protein folding / lipopolysaccharide binding / unfolded protein binding / protein folding / outer membrane-bounded periplasmic space / protein stabilization / identical protein binding / cytosol
Similarity search - Function
Chaperone protein Skp / Skp domain superfamily / Outer membrane protein (OmpH-like) / Outer membrane protein (OmpH-like)
Similarity search - Domain/homology
Chaperone protein Skp
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
CitationDate: 2017 Jun
Title: A Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone
Authors: Holdbrook D / Burmann B / Huber R / Petoukhov M / Svergun D / Hiller S
Contact author
  • Maxim Petoukhov (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #551
Type: mix / Radius of dummy atoms: 1.90 A / Symmetry: P3
Search similar-shape structures of this assembly by Omokage search (details)
Model #552
Type: mix / Radius of dummy atoms: 1.90 A / Symmetry: P3
Search similar-shape structures of this assembly by Omokage search (details)
Model #553
Type: mix / Radius of dummy atoms: 1.90 A / Symmetry: P3
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Trimeric periplasmic holdase chaperone protein Skp / Specimen concentration: 0.58-5.82
BufferName: 25 mM HEPES 150 mM NaCl 1 mM DTT / Concentration: 25.00 mM / pH: 7.5 / Composition: 150 mM NaCl, 1 mM DTT
Entity #354Name: Skp / Type: protein / Description: Periplasmic holdase chaperone protein Skp / Formula weight: 15.692 / Num. of mol.: 3 / Source: Escherichia coli / References: UniProt: P0AEU7
Sequence:
ADKIAIVNMG SLFQQVAQKT GVSNTLENEF KGRASELQRM ETDLQAKMKK LQSMKAGSDR TKLEKDVMAQ RQTFAQKAQA FEQDRARRSN EERGKLVTRI QTAVKSVANS QDIDLVVDAN AVAYNSSDVK DITADVLKQV K

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Experimental information

BeamInstrument name: PETRA III P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron / Wavelength: 0.12 Å / Dist. spec. to detc.: 3.1 mm
DetectorName: Pilatus 2M
Scan
Title: Trimeric periplasmic holdase chaperone protein Skp / Measurement date: Sep 24, 2013 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
MinMax
Q0.0969 4.4372
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 828 /
MinMax
Q0.110109 2.28684
P(R) point1 828
R0 12.8
Result
Type of curve: merged
Comments: The models presented above are representatives from the trimeric ensemble state(s) of Skp as determined using Ensemble Optimization Method (EOM). The Rg and size distributions obtained from ...Comments: The models presented above are representatives from the trimeric ensemble state(s) of Skp as determined using Ensemble Optimization Method (EOM). The Rg and size distributions obtained from EOM modelling are included in the full entry zip archive.
ExperimentalPorod
MW35 kDa100 kDa
Volume-168 nm3

P(R)P(R) errorGuinierGuinier error
Forward scattering, I04369 29.7 4451.7 54.4
Radius of gyration, Rg3.57 nm0.02 3.57 nm0.07

MinMax
D-12.8
Guinier point1 99

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