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- SASDAF5: CYNEX4-T266D (CYNEX4 FRET probe, (eYFP-AnnexinA4-eCFP) T266D mutant) -

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Open data


ID or keywords:

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Basic information

Entry
Database: SASBDB / ID: SASDAF5
SampleCYNEX4-T266D
  • CYNEX4 FRET probe, (eYFP-AnnexinA4-eCFP) T266D mutant (protein), CYNEX4-T266D, Homo sapiens
Biological speciesHomo sapiens (human)
CitationJournal: Biophys J / Year: 2012
Title: Conformational analysis of a genetically encoded FRET biosensor by SAXS.
Authors: Haydyn D T Mertens / Alen Piljić / Carsten Schultz / Dmitri I Svergun /
Abstract: Genetically encoded FRET (Foerster resonance energy transfer) sensors are exciting tools in modern cell biology. Changes in the conformation of a sensor lead to an altered emission ratio and provide ...Genetically encoded FRET (Foerster resonance energy transfer) sensors are exciting tools in modern cell biology. Changes in the conformation of a sensor lead to an altered emission ratio and provide the means to determine both temporal and spatial changes in target molecules, as well as the activity of enzymes. FRET sensors are widely used to follow phosphorylation events and to monitor the effects of elevated calcium levels. Here, we report for the first time, to our knowledge, on the analysis of the conformational changes involved in sensor function at low resolution using a combination of in vitro and in cellulo FRET measurements and small-angle scattering of x rays (SAXS). The large and dynamic structural rearrangements involved in the modification of the calcium- and phosphorylation-sensitive probe CYNEX4 are comprehensively characterized. It is demonstrated that the synergistic use of SAXS and FRET methods allows one to resolve the ambiguities arising due to the rotation of the sensor molecules and the flexibility of the probe.
Contact author
  • Haydyn Mertens (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

Downloads & links

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Models

Model #112
Type: dummy / Software: dammif / Radius of dummy atoms: 2.80 A / Chi-square value: 0.622521
Search similar-shape structures of this assembly by Omokage search (details)
Model #114
Type: mix / Software: coral / Radius of dummy atoms: 1.90 A / Chi-square value: 0.5776
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: CYNEX4-T266D / Sample MW: 92.8 kDa / Specimen concentration: 0.90-17.00 / Concentration method: A280
BufferName: HEPES / Concentration: 50.00 mM / PK: 7 / pH: 7.5 / Comment: 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid / Composition: KCl 50.000 mM
Entity #89Name: CYNEX4-T266D / Type: protein
Description: CYNEX4 FRET probe, (eYFP-AnnexinA4-eCFP) T266D mutant
Formula weight: 92.8 / Num. of mol.: 1 / Source: Homo sapiens
Sequence: MASWSHPQFE KGAMASKGEE LFTGVVPILV ELDGDVNGHK FSVSGEGEGD ATYGKLTLKF ICTTGKLPVP WPTLVTTFSY GVQCFSRYPD HMKRHDFFKS AMPEGYVQER TIFFKDDGNY KTRAEVKFEG DTLVNRIELK GIDFKEDGNI LGHKLEYNYN SHNVYIMADK ...Sequence:
MASWSHPQFE KGAMASKGEE LFTGVVPILV ELDGDVNGHK FSVSGEGEGD ATYGKLTLKF ICTTGKLPVP WPTLVTTFSY GVQCFSRYPD HMKRHDFFKS AMPEGYVQER TIFFKDDGNY KTRAEVKFEG DTLVNRIELK GIDFKEDGNI LGHKLEYNYN SHNVYIMADK QKNGIKVNFK IRHNIEDGSV QLADHYQQNT PIGDGPVLLP DNHYLSTQSA LSKDPNEKRD HMVLLEFVTA AGITLGMDEL YKRILATMAM ATKGGTVKAA SGFNAMEDAQ TLRKAMKGLG TDEDAIISVL AYRNTAQRQE IRTAYKSTIG RDLIDDLKSE LSGNFEQVIV GMMTPTVLYD VQELRRAMKG AGTDEGCLIE ILASRTPEEI RRISQTYQQQ YGRSLEDDIR SDTSFMFQRV LVSLSAGGRD EGNYLDDALV RQDAQDLYEA GEKKWGTDEV KFLTVLCSRN RNHLLHVFDE YKRISQKDIE QSIKSETSGS FEDALLAIVK CMRNKSAYFA EKLYKSMKGL GTDDNTLIRV MVSRAEIDML DIRAHFKRLY GKSLYSFIKG DTSGDYRKVL LVLCGGDDSR DPPVATMASK GEELFTGVVP ILVELDGDVN GHKFSVSGEG EGDATYGKLT LKFICTTGKL PVPWPTLVTT FSYGVQCFSR YPDHMKRHDF FKSAMPEGYV QERTIFFKDD GNYKTRAEVK FEGDTLVNRI ELKGIDFKED GNILGHKLEY NYNSHNVYIM ADKQKNGIKV NFKIRHNIED GSVQLADHYQ QNTPIGDGPV LLPDNHYLST QSALSKDPNE KRDHMVLLEF VTAAGITLGM DELYK

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Experimental information

BeamInstrument name: DORIS III X33 / City: Hamburg / 国: Germany / Shape: 0.6 / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.15 Å / Dist. spec. to detc.: 2.7 mm
DetectorName: Pilatus 1M-W / Pixsize x: 0.172 mm
Scan
Title: cynex4-T266D / Measurement date: Sep 11, 2010 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 15 sec. / Number of frames: 8 / Unit: 1/nm /
MinMax
Q0.1438 6.0155
Distance distribution function P(R)
Sofotware P(R): GNOM 4.5a / Number of points: 322 /
MinMax
Q0.1998 1.957
P(R) point21 342
R0 13.36
Result
Type of curve: merged / Standard: BSA
ExperimentalStandardPorod
MW92.8 kDa96 kDa96 kDa
Volume--146 nm3

GuinierP(R)
Forward scattering, I088 -
Radius of gyration, Rg4.1 nm4.2 nm

MinMax
D-14.4
Guinier point1 63

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