Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural Insight into Phospholipid Transport by the MlaFEBD Complex from P. aeruginosa.
Journal, issue, pages	J Mol Biol, Vol. 433, Issue 13, Page 166986, Year 2021
Publish date	Jun 25, 2021
Authors	Changping Zhou / Huigang Shi / Manfeng Zhang / Lijun Zhou / Le Xiao / Shasha Feng / Wonpil Im / Min Zhou / Xinzheng Zhang / Yihua Huang /
PubMed Abstract	The outer membrane (OM) of Gram-negative bacteria, which consists of lipopolysaccharides (LPS) in the outer leaflet and phospholipids (PLs) in the inner leaflet, plays a key role in antibiotic ...The outer membrane (OM) of Gram-negative bacteria, which consists of lipopolysaccharides (LPS) in the outer leaflet and phospholipids (PLs) in the inner leaflet, plays a key role in antibiotic resistance and pathogen virulence. The maintenance of lipid asymmetry (Mla) pathway is known to be involved in PL transport and contributes to the lipid homeostasis of the OM, yet the underlying molecular mechanism and the directionality of PL transport in this pathway remain elusive. Here, we reported the cryo-EM structures of the ATP-binding cassette (ABC) transporter MlaFEBD from P. areuginosa, the core complex in the Mla pathway, in nucleotide-free (apo)-, ADP (ATP + vanadate)- and ATP (AMPPNP)-bound states as well as the structures of MlaFEB from E. coli in apo- and AMPPNP-bound states at a resolution range of 3.4-3.9 Å. The structures show that the MlaFEBD complex contains a total of twelve protein molecules with a stoichiometry of MlaFEBD, and binds a plethora of PLs at different locations. In contrast to canonical ABC transporters, nucleotide binding fails to trigger significant conformational changes of both MlaFEBD and MlaFEB in the nucleotide-binding and transmembrane domains of the ABC transporter, correlated with their low ATPase activities exhibited in both detergent micelles and lipid nanodiscs. Intriguingly, PLs or detergents appeared to relocate to the membrane-proximal end from the distal end of the hydrophobic tunnel formed by the MlaD hexamer in MlaFEBD upon addition of ATP, indicating that retrograde PL transport might occur in the tunnel in an ATP-dependent manner. Site-specific photocrosslinking experiment confirms that the substrate-binding pocket in the dimeric MlaE and the MlaD hexamer are able to bind PLs in vitro, in line with the notion that MlaFEBD complex functions as a PL transporter.
External links	J Mol Biol / PubMed:33845086
Methods	EM (single particle)
Resolution	3.4 - 3.9 Å
Structure data	30369 7ch6 EMDB-30369, PDB-7ch6: Cryo-EM structure of E.coli MlaFEB with AMPPNP Method: EM (single particle) / Resolution: 3.4 Å 30370 7ch7 EMDB-30370, PDB-7ch7: Cryo-EM structure of E.coli MlaFEB Method: EM (single particle) / Resolution: 3.9 Å 30371 7ch8 EMDB-30371, PDB-7ch8: Cryo-EM structure of P.aeruginosa MlaFEBD with ADP-V Method: EM (single particle) / Resolution: 3.9 Å 30372 7ch9 EMDB-30372, PDB-7ch9: Cryo-EM structure of P.aeruginosa MlaFEBD Method: EM (single particle) / Resolution: 3.5 Å 30373 7cha EMDB-30373, PDB-7cha: Cryo-EM structure of P.aeruginosa MlaFEBD with AMPPNP Method: EM (single particle) / Resolution: 3.9 Å
Chemicals	ChemComp-ANP: PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogueYM ChemComp-LPP: 2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE / phospholipidYM ChemComp-AD9: ADP METAVANADATE ChemComp-MG: Unknown entry
Source	Escherichia coli K12 (bacteria) escherichia coli (strain k12) (bacteria) Escherichia coli K-12 (bacteria) pseudomonas aeruginosa (strain atcc 15692 / dsm 22644 / cip 104116 / jcm 14847 / lmg 12228 / 1c / prs 101 / pao1) (bacteria) pseudomonas aeruginosa pao1 (bacteria)
Keywords	MEMBRANE PROTEIN / Mla complex / Lipid transporter