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5ttp

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Cryo-EM structure of MsbA-nanodisc with ADP-vanadate

5ttp, resolution 4.80Å

Structural highlights

5ttp is a 2 chain structure with sequence from Escherichia coli O157:H7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 4.8Å
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MSBA_ECOLI Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.

Publication Abstract from PubMed

Lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria is critical for the assembly of their cell envelopes. LPS synthesized in the cytoplasmic leaflet of the inner membrane is flipped to the periplasmic leaflet by MsbA, an ATP-binding cassette transporter. Despite substantial efforts, the structural mechanisms underlying MsbA-driven LPS flipping remain elusive. Here we use single-particle cryo-electron microscopy to elucidate the structures of lipid-nanodisc-embedded MsbA in three functional states. The 4.2 A-resolution structure of the transmembrane domains of nucleotide-free MsbA reveals that LPS binds deep inside MsbA at the height of the periplasmic leaflet, establishing extensive hydrophilic and hydrophobic interactions with MsbA. Two sub-nanometre-resolution structures of MsbA with ADP-vanadate and ADP reveal an unprecedented closed and an inward-facing conformation, respectively. Our study uncovers the structural basis for LPS recognition, delineates the conformational transitions of MsbA to flip LPS, and paves the way for structural characterization of other lipid flippases.

Structural basis of MsbA-mediated lipopolysaccharide transport.,Mi W, Li Y, Yoon SH, Ernst RK, Walz T, Liao M Nature. 2017 Sep 14;549(7671):233-237. doi: 10.1038/nature23649. Epub 2017 Sep 6. PMID:28869968^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Mi W, Li Y, Yoon SH, Ernst RK, Walz T, Liao M. Structural basis of MsbA-mediated lipopolysaccharide transport. Nature. 2017 Sep 14;549(7671):233-237. doi: 10.1038/nature23649. Epub 2017 Sep 6. PMID:28869968 doi:http://dx.doi.org/10.1038/nature23649

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ttp"

Categories: Escherichia coli O157:H7 | Large Structures | Liao M | Mi W | Walz T

@@ Line 1: / Line 1: @@
 ==Cryo-EM structure of MsbA-nanodisc with ADP-vanadate==
-<StructureSection load='5ttp' size='340' side='right' caption='[[5ttp]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
+<SX load='5ttp' size='340' side='right' viewer='molstar' caption='[[5ttp]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ttp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TTP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TTP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ttp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TTP FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ttp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ttp OCA], [http://pdbe.org/5ttp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ttp RCSB], [http://www.ebi.ac.uk/pdbsum/5ttp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ttp ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.8&#8491;</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ttp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ttp OCA], [https://pdbe.org/5ttp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ttp RCSB], [https://www.ebi.ac.uk/pdbsum/5ttp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ttp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MSBA_ECO57 MSBA_ECO57]] Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
+[https://www.uniprot.org/uniprot/MSBA_ECOLI MSBA_ECOLI] Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 21: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
-[[Category: Liao, M]]
+[[Category: Escherichia coli O157:H7]]
-[[Category: Mi, W]]
+[[Category: Large Structures]]
-[[Category: Walz, T]]
+[[Category: Liao M]]
-[[Category: Abc transporter]]
+[[Category: Mi W]]
-[[Category: Flippase]]
+[[Category: Walz T]]
-[[Category: Hydrolase]]
-[[Category: Lp]]
-[[Category: Nanodisc]]

5ttp

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Current revision

Cryo-EM structure of MsbA-nanodisc with ADP-vanadate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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