Cryo-EM structure of the glucose-specific PTS transporter IICB from E. coli in the inward- and outward-facing conformation. Determined by electron microscopy at 2.89 Å resolution. Released 25 Sept 2024.
Explore 8QST in 3D Show helices and sheets RCSB PDB PDBe
8QST contains 52 α-helices and 6 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-15 | 10 | |
| α-helix | 17-21 | 5 | |
| α-helix | 23-34 | 12 | |
| α-helix | 47-70 | 24 | |
| α-helix | 76-101 | 26 | |
| α-helix | 107-111 | 5 | |
| α-helix | 118-135 | 18 | |
| α-helix | 142-147 | 6 | |
| α-helix | 149-151 | 3 | |
| α-helix | 153-168 | 16 | |
| α-helix | 173-181 | 9 | |
| α-helix | 185-188 | 4 | |
| α-helix | 191-205 | 15 | |
| α-helix | 206-208 | 3 | |
| α-helix | 211-216 | 6 | |
| α-helix | 217-221 | 5 | |
| β-strand | 225 | 1 | 1 |
| α-helix | 231-232 | 2 | |
| β-strand | 233 | 1 | 1 |
| α-helix | 236-241 | 6 | |
| α-helix | 253-254 | 2 | |
| α-helix | 255-260 | 6 | |
| α-helix | 261-269 | 9 | |
| α-helix | 277-294 | 18 | |
| α-helix | 298-304 | 7 | |
| α-helix | 309-329 | 21 | |
| α-helix | 341-346 | 6 | |
| α-helix | 356-379 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-20 | 16 | |
| α-helix | 23-26 | 4 | |
| α-helix | 27-31 | 5 | |
| α-helix | 32-34 | 3 | |
| α-helix | 42-57 | 16 | |
| α-helix | 59-70 | 12 | |
| α-helix | 76-101 | 26 | |
| α-helix | 105-111 | 7 | |
| α-helix | 118-135 | 18 | |
| α-helix | 142-144 | 3 | |
| α-helix | 149-151 | 3 | |
| α-helix | 152-184 | 33 | |
| α-helix | 185-189 | 5 | |
| α-helix | 191-205 | 15 | |
| α-helix | 211-220 | 10 | |
| β-strand | 225-226 | 2 | 2 |
| β-strand | 232-233 | 2 | 2 |
| α-helix | 237-242 | 6 | |
| α-helix | 249-252 | 4 | |
| α-helix | 253-254 | 2 | |
| α-helix | 255-260 | 6 | |
| α-helix | 261-270 | 10 | |
| α-helix | 274-276 | 3 | |
| α-helix | 277-293 | 17 | |
| α-helix | 298-304 | 7 | |
| α-helix | 309-329 | 21 | |
| β-strand | 332 | 1 | 3 |
| α-helix | 341-346 | 6 | |
| β-strand | 352 | 1 | 3 |
| α-helix | 356-379 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| PTS system glucose-specific EIICB component | A, B | protein | 499 | Escherichia coli | P69786 (AlphaFold model) |
>8QST_1 PTS system glucose-specific EIICB component (chains A, B) MFKNAFANLQKVGKSLMLPVSVLPIAGILLGVGSANFSWLPAVVSHVMAEAGGSVFANMP LIFAIGVALGFTNNDGVSALAAVVAYGIMVKTMAVVAPLVLHLPAEEIASKHLADTGVLG GIISGAIAAYMFNRFYRIKLPEYLGFFAGKRFVPIISGLAAIFTGVVLSFIWPPIGSAIQ TFSQWAAYQNPVVAFGIYGFIERCLVPFGLHHIWNVPFQMQIGEYTNAAGQVFHGDIPRY MAGDPTAGKLSGGFLFKMYGLPAAAIAIWHSAKPENRAKVGGIMISAALTSFLTGITEPI EFSFMFVAPILYIIHAILAGLAFPICILLGMRDGTSFSHGLIDFIVLSGNSSKLWLFPIV GIGYAIVYYTIFRVLIKALDLKTPGREDATEDAKATGTSEMAPALVAAFGGKENITNLDA CITRLRVSVADVSKVDQAGLKKLGAAGVVVAGSGVQAIFGTKSDNLKTEMDEYIRNHLEL EVLFQGPVDHHHHHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| BGC | beta-D-glucopyranose | C6 H12 O6 | 2 |
Structure and mechanism of a phosphotransferase system glucose transporter. Roth, P., Jeckelmann, J.M., Fender, I. et al. Nat Commun (2024) 15:7992-7992. DOI 10.1038/s41467-024-52100-3 · PubMed
Other PDB entries of the same protein (UniProt P69786 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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