LolCDE with bound RcsF in nanodiscs. Determined by electron microscopy at 3.5 Å resolution. Released 21 Sept 2022.
Explore 7V8L in 3D Show helices and sheets RCSB PDB PDBe
7V8L contains 57 α-helices and 44 β-strands across 4 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 | 5-13 | 9 | |
| α-helix | 23-27 | 5 | |
| α-helix | 29-58 | 30 | |
| α-helix | 60-62 | 3 | |
| β-strand | 66-70 | 5 | 3 |
| β-strand | 75 | 1 | 4 |
| α-helix | 82-84 | 3 | |
| β-strand | 90-96 | 7 | 3 |
| β-strand | 97-104 | 8 | 5 |
| β-strand | 109-117 | 9 | 5 |
| α-helix | 126-128 | 3 | |
| β-strand | 129-130 | 2 | 5 |
| α-helix | 134-136 | 3 | |
| β-strand | 143-147 | 5 | 5 |
| α-helix | 148-154 | 7 | |
| β-strand | 161-173 | 13 | 5 |
| β-strand | 176-190 | 15 | 5 |
| α-helix | 195-198 | 4 | |
| β-strand | 200-204 | 5 | 5 |
| α-helix | 205-211 | 7 | |
| α-helix | 214-215 | 2 | |
| β-strand | 219 | 1 | 4 |
| β-strand | 221-226 | 6 | 3 |
| α-helix | 229-231 | 3 | |
| α-helix | 232-235 | 4 | |
| β-strand | 244-248 | 5 | 3 |
| α-helix | 250-270 | 21 | |
| α-helix | 272-302 | 31 | |
| α-helix | 307-336 | 30 | |
| α-helix | 340-343 | 4 | |
| α-helix | 362-389 | 28 | |
| α-helix | 392-396 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-12 | 6 | 6 |
| β-strand | 39-41 | 3 | 7 |
| α-helix | 49-55 | 7 | |
| β-strand | 63-68 | 6 | 6 |
| β-strand | 71-72 | 2 | 6 |
| α-helix | 78-83 | 6 | |
| α-helix | 84-88 | 5 | |
| β-strand | 89-91 | 3 | 7 |
| α-helix | 104-114 | 11 | |
| α-helix | 119-133 | 15 | |
| α-helix | 143-145 | 3 | |
| α-helix | 148-159 | 12 | |
| β-strand | 166-170 | 5 | 7 |
| α-helix | 178-190 | 13 | |
| α-helix | 191-195 | 5 | |
| β-strand | 198-202 | 5 | 7 |
| α-helix | 206-210 | 5 | |
| β-strand | 214-219 | 6 | 7 |
| β-strand | 222-228 | 7 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-8 | 3 | |
| α-helix | 9-15 | 7 | |
| α-helix | 25-54 | 30 | |
| α-helix | 55-59 | 5 | |
| β-strand | 66-69 | 4 | 1 |
| α-helix | 78-86 | 9 | |
| β-strand | 91-97 | 7 | 1 |
| β-strand | 98-106 | 9 | 2 |
| β-strand | 109-117 | 9 | 2 |
| α-helix | 120-126 | 7 | |
| α-helix | 129-132 | 4 | |
| β-strand | 133 | 1 | 2 |
| β-strand | 147-151 | 5 | 2 |
| α-helix | 152-157 | 6 | |
| β-strand | 165-170 | 6 | 2 |
| α-helix | 177-179 | 3 | |
| β-strand | 183-193 | 11 | 2 |
| α-helix | 199-201 | 3 | |
| β-strand | 204-206 | 3 | 2 |
| α-helix | 208-215 | 8 | |
| β-strand | 223-228 | 6 | 1 |
| α-helix | 234-244 | 11 | |
| β-strand | 250-253 | 4 | 1 |
| α-helix | 254-297 | 44 | |
| α-helix | 299-306 | 8 | |
| α-helix | 314-340 | 27 | |
| α-helix | 345-355 | 11 | |
| α-helix | 377-403 | 27 | |
| α-helix | 407-411 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-12 | 6 | 8 |
| β-strand | 38-41 | 4 | 9 |
| α-helix | 49-55 | 7 | |
| β-strand | 63-68 | 6 | 8 |
| β-strand | 71-72 | 2 | 8 |
| α-helix | 78-83 | 6 | |
| α-helix | 84-88 | 5 | |
| β-strand | 89-92 | 4 | 9 |
| α-helix | 104-114 | 11 | |
| α-helix | 119-133 | 15 | |
| α-helix | 135-137 | 3 | |
| α-helix | 148-159 | 12 | |
| β-strand | 166-170 | 5 | 9 |
| α-helix | 178-190 | 13 | |
| α-helix | 191-195 | 5 | |
| β-strand | 198-202 | 5 | 9 |
| α-helix | 206-209 | 4 | |
| β-strand | 214-217 | 4 | 9 |
| β-strand | 219 | 1 | 10 |
| β-strand | 222 | 1 | 10 |
| β-strand | 226-228 | 3 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lipoprotein-releasing system transmembrane protein LolE | E | protein | 414 | Escherichia coli K-12 | P75958 (AlphaFold model) |
| Outer membrane lipoprotein RcsF | A | protein | 118 | Escherichia coli K-12 | P69411 (AlphaFold model) |
| Lipoprotein-releasing system transmembrane protein LolC | C | protein | 399 | Escherichia coli K-12 | P0ADC3 (AlphaFold model) |
| Lipoprotein-releasing system ATP-binding protein LolD | D, F | protein | 233 | Escherichia coli K-12 | P75957 (AlphaFold model) |
>7V8L_1 Lipoprotein-releasing system transmembrane protein LolE (chains E) MAMPLSLLIGLRFSRGRRRGGMVSLISVISTIGIALGVAVLIVGLSAMNGFERELNNRIL AVVPHGEIEAVDQPWTNWQEALDHVQKVPGIAAAAPYINFTGLVESGANLRAIQVKGVNP QQEQRLSALPSFVQGDAWRNFKAGEQQIIIGKGVADALKVKQGDWVSIMIPNSNPEHKLM QPKRVRLHVAGILQLSGQLDHSFAMIPLADAQQYLDMGSSVSGIALKMTDVFNANKLVRD AGEVTNSYVYIKSWIGTYGYMYRDIQMIRAIMYLAMVLVIGVACFNIVSTLVMAVKDKSG DIAVLRTLGAKDGLIRAIFVWYGLLAGLFGSLCGVIIGVVVSLQLTPIIEWIEKLIGHQF LSSDIYFIDFLPSELHWLDVFYVLVTALLLSLLASWYPARRASNIDPARVLSGQ
>7V8L_2 Outer membrane lipoprotein RcsF (chains A) SMLSRSPVEPVQSTAPQPKAEPAKPKAPRATPVRIYTNAEELVGKPFRDLGEVSGDSCQA SNQDSPPSIPTARKRMQINASKMKANAVLLHSCEVTSGTPGCYRQAVCIGSALNITAK
>7V8L_3 Lipoprotein-releasing system transmembrane protein LolC (chains C) MYQPVALFIGLRYMRGRAADRFGRFVSWLSTIGITLGVMALVTVLSVMNGFERELQNNIL GLMPQAILSSEHGSLNPQQLPETAVKLDGVNRVAPITTGDVVLQSARSVAVGVMLGIDPA QKDPLTPYLVNVKQTDLEPGKYNVILGEQLASQLGVNRGDQIRVMVPSASQFTPMGRIPS QRLFNVIGTFAANSEVDGYEMLVNIEDASRLMRYPAGNITGWRLWLDEPLKVDSLSQQKL PEGSKWQDWRDRKGELFQAVRMEKNMMGLLLSLIVAVAAFNIITSLGLMVMEKQGEVAIL QTQGLTPRQIMMVFMVQGASAGIIGAILGAALGALLASQLNNLMPIIGVLLDGAALPVAI EPLQVIVIALVAMAIALLSTLYPSWRAAATQPAEALRYE
>7V8L_4 Lipoprotein-releasing system ATP-binding protein LolD (chains D, F) MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDT PTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPA EINSRALEMLKAVGLDHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAE
| ID | Name | Formula | Copies |
|---|---|---|---|
| PCJ | (2R)-3-{[(2S)-3-hydroxy-2-(palmitoylamino)propyl]thio}propane-1,2-diyl… | C54 H105 N O6 S | 1 |
Cryo-EM structures of LolCDE reveal the molecular mechanism of bacterial lipoprotein sorting in Escherichia coli. Bei, W., Luo, Q., Shi, H. et al. PLoS Biol (2022) 20:e3001823-e3001823. DOI 10.1371/journal.pbio.3001823 · PubMed
Other PDB entries of the same protein (UniProt P75958 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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