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- SASDDD5: MsbA in stealth nanodisc (SAXS) (Lipid A export ATP-binding/perme... -

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Basic information

Entry
Database: SASBDB / ID: SASDDD5
SampleMsbA in stealth nanodisc (SAXS)
  • Lipid A export ATP-binding/permease protein MsbA (protein), MsbA, Escherichia coli (strain K12)
  • Membrane scaffold protein 1D1 (deuterated, 75%) (protein), d75-msp1d1
  • 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) (other), d(78,92)-POPC, Escherichia coli. (AL95 strain)
Function / homology
Function and homology information


MsbA transporter complex / lipopolysaccharide floppase activity / lipid translocation / ABC-type lipid A-core oligosaccharide transporter / lipopolysaccharide transport / ATPase-coupled lipid transmembrane transporter activity / ABC-type xenobiotic transporter activity / lipid transport / ATP-binding cassette (ABC) transporter complex / transmembrane transport ...MsbA transporter complex / lipopolysaccharide floppase activity / lipid translocation / ABC-type lipid A-core oligosaccharide transporter / lipopolysaccharide transport / ATPase-coupled lipid transmembrane transporter activity / ABC-type xenobiotic transporter activity / lipid transport / ATP-binding cassette (ABC) transporter complex / transmembrane transport / lipid binding / ATP hydrolysis activity / ATP binding / identical protein binding / membrane / plasma membrane
Similarity search - Function
Lipid A export ATP-binding/permease protein msbA family profile. / ABC transporter, lipid A-core flippase, MsbA / Type 1 protein exporter / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter ...Lipid A export ATP-binding/permease protein msbA family profile. / ABC transporter, lipid A-core flippase, MsbA / Type 1 protein exporter / ABC transporter transmembrane region / ABC transporter type 1, transmembrane domain / ABC transporter integral membrane type-1 fused domain profile. / ABC transporter type 1, transmembrane domain superfamily / ABC transporter-like, conserved site / ABC transporters family signature. / ABC transporter / ABC transporter-like, ATP-binding domain / ATP-binding cassette, ABC transporter-type domain profile. / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ATP-dependent lipid A-core flippase
Similarity search - Component
Biological speciesEscherichia coli (strain K12) (bacteria)
Escherichia coli. (AL95 strain)
CitationJournal: Structure / Year: 2018
Title: Conformational States of ABC Transporter MsbA in a Lipid Environment Investigated by Small-Angle Scattering Using Stealth Carrier Nanodiscs.
Authors: Inokentijs Josts / Julius Nitsche / Selma Maric / Haydyn D Mertens / Martine Moulin / Michael Haertlein / Sylvain Prevost / Dmitri I Svergun / Sebastian Busch / V Trevor Forsyth / Henning Tidow /
Abstract: Structural studies of integral membrane proteins (IMPs) are challenging, as many of them are inactive or insoluble in the absence of a lipid environment. Here, we describe an approach making use of ...Structural studies of integral membrane proteins (IMPs) are challenging, as many of them are inactive or insoluble in the absence of a lipid environment. Here, we describe an approach making use of fractionally deuterium labeled "stealth carrier" nanodiscs that are effectively invisible to low-resolution neutron diffraction and enable structural studies of IMPs in a lipidic native-like solution environment. We illustrate the potential of the method in a joint small-angle neutron scattering (SANS) and X-ray scattering (SAXS) study of the ATP-binding cassette (ABC) transporter protein MsbA solubilized in the stealth nanodiscs. The data allow for a direct observation of the signal from the solubilized protein without contribution from the surrounding lipid nanodisc. Not only the overall shape but also differences between conformational states of MsbA can be reliably detected from the scattering data, demonstrating the sensitivity of the approach and its general applicability to structural studies of IMPs.
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

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Models

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Sample

SampleName: MsbA in stealth nanodisc (SAXS) / Contrast: 2.644 / Specific vol: 0.745 / Specimen concentration: 1.00-2.70 / Concentration method: A280 / Entity id: 1016 / 1017 / 1018
BufferName: 30 mM Tris, 150 mM NaCl / pH: 7.5 / Comment: nanodisc buffer
Entity #1016Name: MsbA / Type: protein
Description: Lipid A export ATP-binding/permease protein MsbA
Formula weight: 66.279 / Num. of mol.: 2 / Source: Escherichia coli (strain K12) / References: UniProt: P60752
Sequence: MHHHHHHGEN LYFQGSHNDK DLSTWQTFRR LWPTIAPFKA GLIVAGVALI LNAASDTFML SLLKPLLDDG FGKTDRSVLV WMPLVVIGLM ILRGITSYVS SYCISWVSGK VVMTMRRRLF GHMMGMPVSF FDKQSTGTLL SRITYDSEQV ASSSSGALIT VVREGASIIG ...Sequence:
MHHHHHHGEN LYFQGSHNDK DLSTWQTFRR LWPTIAPFKA GLIVAGVALI LNAASDTFML SLLKPLLDDG FGKTDRSVLV WMPLVVIGLM ILRGITSYVS SYCISWVSGK VVMTMRRRLF GHMMGMPVSF FDKQSTGTLL SRITYDSEQV ASSSSGALIT VVREGASIIG LFIMMFYYSW QLSIILIVLA PIVSIAIRVV SKRFRNISKN MQNTMGQVTT SAEQMLKGHK EVLIFGGQEV ETKRFDKVSN RMRLQGMKMV SASSISDPII QLIASLALAF VLYAASFPSV MDSLTAGTIT VVFSSMIALM RPLKSLTNVN AQFQRGMAAC QTLFTILDSE QEKDEGKRVI ERATGDVEFR NVTFTYPGRD VPALRNINLK IPAGKTVALV GRSGSGKSTI ASLITRFYDI DEGEILMDGH DLREYTLASL RNQVALVSQN VHLFNDTVAN NIAYARTEQY SREQIEEAAR MAYAMDFINK MDNGLDTVIG ENGVLLSGGQ RQRIAIARAL LRDSPILILD EATSALDTES ERAIQAALDE LQKNRTSLVI AHRLSTIEKA DEIVVVEDGV IVERGTHNDL LEHRGVYAQL HKMQFGQ
Entity #1017Name: d75-msp1d1 / Type: protein
Description: Membrane scaffold protein 1D1 (deuterated, 75%)
Formula weight: 24.661 / Num. of mol.: 2
Sequence: GHHHHHHHDY DIPTTENLYF QGSTFSKLRE QLGPVTQEFW DNLEKETEGL RQEMSKDLEE VKAKVQPYLD DFQKKWQEEM ELYRQKVEPL RAELQEGARQ KLHELQEKLS PLGEEMRDRA RAHVDALRTH LAPYSDELRQ RLAARLEALK ENGGARLAEY HAKATEHLST ...Sequence:
GHHHHHHHDY DIPTTENLYF QGSTFSKLRE QLGPVTQEFW DNLEKETEGL RQEMSKDLEE VKAKVQPYLD DFQKKWQEEM ELYRQKVEPL RAELQEGARQ KLHELQEKLS PLGEEMRDRA RAHVDALRTH LAPYSDELRQ RLAARLEALK ENGGARLAEY HAKATEHLST LSEKAKPALE DLRQGLLPVL ESFKVSFLSA LEEYTKKLNT Q
Entity #1018Name: d(78,92)-POPC / Type: other
Description: 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)
Formula weight: 0.76 / Source: Escherichia coli. (AL95 strain)
Sequence:
C42H82NO8P

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Experimental information

BeamInstrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotron / Wavelength: 0.124 Å / Dist. spec. to detc.: 3.3 mm
DetectorName: Pilatus 2M
Scan
Title: MsbA in stealth nanodisc / Measurement date: Sep 8, 2017 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /
MinMax
Q0.0249 5.064
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 781 /
MinMax
Q0.0332076 2.18572
P(R) point1 781
R0 16
Result
Type of curve: single_conc / Standard: water
Comments: 'MsbA ABC transporter protein encapsulated in a partially deuterated
ExperimentalExperimental errorPorodPorod error
MW206.6 kDa20 379 kDa40
Volume--607 nm360

P(R)P(R) errorGuinierGuinier error
Forward scattering, I00.13 0.003 0.125 0.003
Radius of gyration, Rg4.75 nm0.1 4.78 nm0.2

MinMaxError
D-16 0.5
Guinier point10 80 -

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