7CH6: E.coli MlaFEB with AMPPNP

Cryo-EM structure of E.coli MlaFEB with AMPPNP. Determined by electron microscopy at 3.4 Å resolution. Released 4 Aug 2021.

Method
Electron microscopy
Resolution
3.4 Å
Organism
Escherichia coli (strain K12)
Chains
6
Atoms
9,260
Mol. weight
136.42 kDa
Ligands
ANP
Released
4 Aug 2021

Explore 7CH6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7CH6 contains 68 α-helices and 34 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and B: 18 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix14-185
α-helix19-2810
α-helix41-477
α-helix48-536
α-helix56-7823
α-helix79-813
α-helix87-959
α-helix99-11416
α-helix117-1204
α-helix128-1336
α-helix1391
α-helix140-1445
α-helix145-1517
α-helix155-17117
α-helix172-1776
α-helix190-1923
α-helix196-21621
α-helix228-25831
Chains C and D: 12 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand7-1481
β-strand27-3261
β-strand37-4042
α-helix47-548
β-strand65-6731
β-strand7111
α-helix79-846
β-strand88-9032
α-helix103-1064
α-helix108-1136
α-helix118-13215
α-helix147-15812
β-strand166-16942
α-helix177-19317
β-strand199-20242
α-helix205-2084
β-strand215-21842
β-strand223-22532
α-helix229-2324
α-helix238-2458
α-helix256-2572
α-helix262-2654
Chains E and F: 4 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand5-955
β-strand1316
β-strand14-1855
α-helix26-305
α-helix32-354
β-strand4116
β-strand42-4327
β-strand4715
α-helix52-6716
β-strand74-7527
α-helix79-879

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Lipid asymmetry maintenance ABC transporter permease subunit MlaEA, Bprotein260Escherichia coli (strain K12)P64606 (AlphaFold model)
Phospholipid ABC transporter ATP-binding protein MlaFC, Dprotein269Escherichia coli (strain K12)P63386 (AlphaFold model)
Lipid asymmetry maintenance protein MlaBE, Fprotein97Escherichia coli (strain K12)P64602 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>7CH6_1 Lipid asymmetry maintenance ABC transporter permease subunit MlaE (chains A, B)
MLLNALASLGHKGIKTLRTFGRAGLMLFNALVGKPEFRKHAPLLVRQLYNVGVLSMLIIV
VSGVFIGMVLGLQGYLVLTTYSAETSLGMLVALSLLRELGPVVAALLFAGRAGSALTAEI
GLMRATEQLSSMEMMAVDPLRRVISPRFWAGVISLPLLTVIFVAVGIWGGSLVGVSWKGI
DSGFFWSAMQNAVDWRMDLVNCLIKSVVFAITVTWISLFNGYDAIPTSAGISRATTRTVV
HSSLAVLGLDFVLTALMFGN
Sequence of entity 2 (C, D), FASTA
>7CH6_2 Phospholipid ABC transporter ATP-binding protein MlaF (chains C, D)
MEQSVANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP
DHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPL
LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM
GVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRV
RQFLDGIADGPVPFRYPAGDYHADLLPGS
Sequence of entity 3 (E, F), FASTA
>7CH6_3 Lipid asymmetry maintenance protein MlaB (chains E, F)
MSESLSWMQTGDTLALSGELDQDVLLPLWEMREEAVKGITCIDLSRVSRVDTGGLALLLH
LIDLAKKQGNNVTLQGVNDKVYTLAKLYNLPADVLPR

Ligands and cofactors

IDNameFormulaCopies
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P32

Primary citation

Structural Insight into Phospholipid Transport by the MlaFEBD Complex from P. aeruginosa. Zhou, C., Shi, H., Zhang, M. et al. J Mol Biol (2021) 433:166986-166986. DOI 10.1016/j.jmb.2021.166986 · PubMed

Other PDB entries of the same protein (UniProt P64606 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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