6ZYE: YnaI in an open-like conformation

YnaI in an open-like conformation. Determined by electron microscopy at 4.1 Å resolution. Released 25 Nov 2020.

Method
Electron microscopy
Resolution
4.1 Å
Organism
Escherichia coli (strain K12)
Chains
7
Atoms
11,592
Mol. weight
300.49 kDa
Released
25 Nov 2020

Explore 6ZYE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6ZYE contains 56 α-helices and 84 β-strands across 7 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, B, C, D, E, F and G: 8 helices, 12 β-strands

ElementResiduesLengthSheet
α-helix-34--1718
α-helix150-15910
α-helix161-17515
β-strand184-18631
β-strand193-19861
β-strand203-20861
β-strand213-21751
α-helix218-2236
β-strand226-22721
α-helix229-2313
β-strand235-24395
α-helix245-2506
α-helix251-26313
β-strand26815
β-strand274-27525
β-strand278-28255
β-strand285-294105
α-helix299-32022
β-strand32415
β-strand328-33253

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
YnaI,Low conductance mechanosensitive channel YnaIA, B, C, D, E, F, Gprotein387Escherichia coli (strain K12)P0AEB5 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G), FASTA
>6ZYE_1 YnaI,Low conductance mechanosensitive channel YnaI (chains A, B, C, D, E, F, G)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXMIAELFTNNALNLVIIFGSCAALI
LMSFWFRRGNRKRKGFLFHAVQFLIYTIIISAVGSIINYVIENYKLKFITPGVIDFICTS
LIAVILTIKLFLLINQFEKQQIKKGRDITSARIMSRIIKITIIVVLVLLYGEHFGMSLSG
LLTFGGIGGLAVGMAGKDILSNFFSGIMLYFDRPFSIGDWIRSPDRNIEGTVAEIGWRIT
KITTFDNRPLYVPNSLFSSISVENPGRMTNRRITTTIGLRYEDAAKVGVIVEAVREMLKN
HPAIDQRQTLLVYFNQFADSSLNIMVYCFTKTTVWAEWLAAQQDVYLKIIDIVQSHGADF
AFPSQTLYMDNITPPEQGRLEHHHHHH

Primary citation

The MscS-like channel YnaI has a gating mechanism based on flexible pore helices. Flegler, V.J., Rasmussen, A., Rao, S. et al. Proc Natl Acad Sci U S A (2020) 117:28754-28762. DOI 10.1073/pnas.2005641117 · PubMed

Other PDB entries of the same protein (UniProt P0AEB5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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