7CH7: E.coli MlaFEB

Cryo-EM structure of E.coli MlaFEB. Determined by electron microscopy at 3.9 Å resolution. Released 19 May 2021.

Method
Electron microscopy
Resolution
3.9 Å
Organism
Escherichia coli (strain K12)
Chains
6
Atoms
9,198
Mol. weight
135.41 kDa
Released
19 May 2021

Explore 7CH7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7CH7 contains 63 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.

Chain A: 17 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix14-185
α-helix19-2810
α-helix40-478
α-helix48-547
α-helix56-7823
α-helix87-948
α-helix95-995
α-helix100-11112
α-helix117-12610
α-helix128-1347
α-helix1391
α-helix140-1445
α-helix145-17127
α-helix172-1776
α-helix190-1923
α-helix196-22328
α-helix231-25828
Chain B: 16 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix14-185
α-helix19-2810
α-helix40-478
α-helix48-547
α-helix56-7823
α-helix87-9711
α-helix100-11112
α-helix117-12610
α-helix128-1347
α-helix1391
α-helix140-1445
α-helix145-17127
α-helix172-1776
α-helix190-1923
α-helix196-22328
α-helix231-25828
Chains C and D: 11 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand7-1481
β-strand1512
β-strand27-3261
β-strand37-4043
α-helix47-548
β-strand6212
β-strand65-6731
β-strand7111
α-helix79-846
β-strand90-9123
α-helix102-11312
α-helix118-13215
α-helix135-1373
α-helix147-15913
β-strand167-16933
α-helix177-19115
β-strand199-20243
α-helix205-2084
β-strand215-21953
β-strand222-22763
α-helix229-2335
α-helix238-2458
α-helix256-2572
Chains E and F: 4 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand5-957
β-strand13-1867
α-helix26-294
α-helix32-354
β-strand41-4337
β-strand4717
α-helix52-6514
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
>7CH7_1 Lipid asymmetry maintenance ABC transporter permease subunit MlaE (chains A, B)
MLLNALASLGHKGIKTLRTFGRAGLMLFNALVGKPEFRKHAPLLVRQLYNVGVLSMLIIV
VSGVFIGMVLGLQGYLVLTTYSAETSLGMLVALSLLRELGPVVAALLFAGRAGSALTAEI
GLMRATEQLSSMEMMAVDPLRRVISPRFWAGVISLPLLTVIFVAVGIWGGSLVGVSWKGI
DSGFFWSAMQNAVDWRMDLVNCLIKSVVFAITVTWISLFNGYDAIPTSAGISRATTRTVV
HSSLAVLGLDFVLTALMFGN
Sequence of entity 2 (C, D), FASTA
>7CH7_2 Phospholipid ABC transporter ATP-binding protein MlaF (chains C, D)
MEQSVANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP
DHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPL
LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM
GVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRV
RQFLDGIADGPVPFRYPAGDYHADLLPGS
Sequence of entity 3 (E, F), FASTA
>7CH7_3 Lipid asymmetry maintenance protein MlaB (chains E, F)
MSESLSWMQTGDTLALSGELDQDVLLPLWEMREEAVKGITCIDLSRVSRVDTGGLALLLH
LIDLAKKQGNNVTLQGVNDKVYTLAKLYNLPADVLPR

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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