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- SASDAY5: Free endophilin (Endophilin-A1 BAR domain, Endophilin) -

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Basic information

Entry
Database: SASBDB / ID: SASDAY5
SampleFree endophilin
  • Endophilin-A1 BAR domain (protein), Endophilin, Mus musculus
Biological speciesMus musculus (house mouse)
CitationJournal: Front Mol Biosci / Year: 2014
Title: Endophilin-A1 BAR domain interaction with arachidonyl CoA.
Authors: Maxim V Petoukhov / Winfried Weissenhorn / Dmitri I Svergun /
Abstract: Endophilin-A1 belongs to the family of BAR domain containing proteins that catalyze membrane remodeling processes via sensing, inducing and stabilizing membrane curvature. We show that the BAR domain ...Endophilin-A1 belongs to the family of BAR domain containing proteins that catalyze membrane remodeling processes via sensing, inducing and stabilizing membrane curvature. We show that the BAR domain of endophilin-A1 binds arachidonic acid and molds its coenzyme A (CoA) activated form, arachidonyl-CoA into a defined structure. We studied low resolution structures of endophilin-A1-BAR and its complex with arachidonyl-CoA in solution using synchrotron small-angle X-ray scattering (SAXS). The free endophilin-A1-BAR domain is shown to be dimeric at lower concentrations but builds tetramers and higher order complexes with increasing concentrations. Extensive titration SAXS studies revealed that the BAR domain produces a homogenous complex with the lipid micelles. The structural model of the complexes revealed two arachidonyl-CoA micelles bound to the distal arms of an endophilin-A1-BAR dimer. Intriguingly, the radius of the bound micelles significantly decreases compared to that of the free micelles, and this structural result may provide hints on the potential biological relevance of the endophilin-A1-BAR interaction with arachidonyl CoA.
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

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MolmilJmol/JSmol

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Models

Model #144
Type: mix / Software: Coral / Radius of dummy atoms: 1.90 A / Chi-square value: 2.531281
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Free endophilin / Sample MW: 58 kDa
BufferName: TRIS-HCL / Concentration: 50.00 mM / pH: 8 / Composition: NaCl 300.000 mM
Entity #105Name: Endophilin / Type: protein / Description: Endophilin-A1 BAR domain / Formula weight: 29 / Num. of mol.: 2 / Source: Mus musculus
Sequence: MSVAGLKKQF HKATQKVSEK VGGAEGTKLD DDFKEMERKV DVTSRAVMEI MTKTIEYLQP NPASRAKLSM INTMSKIRGQ EKGPGYPQAE ALLAEAMLKF GRELGDDCNF GPALGEVGEA MRELSEVKDS LDMEVKQNFI DPLQNLHDKD LREIQHHLKK LEGRRLDFDY ...Sequence:
MSVAGLKKQF HKATQKVSEK VGGAEGTKLD DDFKEMERKV DVTSRAVMEI MTKTIEYLQP NPASRAKLSM INTMSKIRGQ EKGPGYPQAE ALLAEAMLKF GRELGDDCNF GPALGEVGEA MRELSEVKDS LDMEVKQNFI DPLQNLHDKD LREIQHHLKK LEGRRLDFDY KKKRQGKIPD EELRQALEKF DESKEIAESS MFNLLEMDIE QVSQLSALVQ AQLEYHKQAV QILQQVTVRL EERIRQA

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Experimental information

BeamInstrument name: DORIS III X33 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron
DetectorName: MAR 345 Image Plate
Scan
Title: endophilin alone / Measurement date: Feb 13, 2004 / Unit: 1/nm /
MinMax
Q0.1579 4.4423
ResultI0 from Guinier: 71.09 / Rg from Guinier: 3.3 nm / D max: 13.5 / Type of curve: merged /
ExperimentalPorod
MW50 kDa-
Volume-90 nm3

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