LolCDE apo structure. Determined by electron microscopy at 3.4 Å resolution. Released 7 Apr 2021.
Explore 7ARI in 3D Show helices and sheets RCSB PDB PDBe
7ARI contains 44 α-helices and 53 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 | 8-13 | 6 | |
| α-helix | 23-54 | 32 | |
| β-strand | 66-67 | 2 | 1 |
| β-strand | 75 | 1 | 2 |
| β-strand | 95-96 | 2 | 3 |
| β-strand | 100-104 | 5 | 4 |
| β-strand | 109-117 | 9 | 4 |
| β-strand | 143-144 | 2 | 5 |
| β-strand | 145 | 1 | 4 |
| β-strand | 146-147 | 2 | 5 |
| α-helix | 148-154 | 7 | |
| β-strand | 160 | 1 | 5 |
| β-strand | 163-166 | 4 | 4 |
| β-strand | 180-183 | 4 | 4 |
| β-strand | 185-190 | 6 | 5 |
| β-strand | 200-204 | 5 | 4 |
| β-strand | 219 | 1 | 2 |
| β-strand | 221-222 | 2 | 3 |
| β-strand | 223-224 | 2 | 1 |
| α-helix | 233-235 | 3 | |
| α-helix | 255-257 | 3 | |
| α-helix | 261-265 | 5 | |
| α-helix | 266-270 | 5 | |
| α-helix | 274-278 | 5 | |
| α-helix | 280-287 | 8 | |
| α-helix | 294-302 | 9 | |
| α-helix | 307-323 | 17 | |
| α-helix | 326-335 | 10 | |
| α-helix | 362-364 | 3 | |
| α-helix | 366-379 | 14 | |
| α-helix | 382-386 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-7 | 2 | 14 |
| β-strand | 16 | 1 | 15 |
| β-strand | 21 | 1 | 15 |
| β-strand | 31-32 | 2 | 14 |
| β-strand | 39-41 | 3 | 16 |
| α-helix | 48-56 | 9 | |
| β-strand | 67 | 1 | 17 |
| β-strand | 68 | 1 | 14 |
| β-strand | 72 | 1 | 17 |
| α-helix | 80-87 | 8 | |
| β-strand | 89-92 | 4 | 16 |
| α-helix | 104-108 | 5 | |
| α-helix | 110-114 | 5 | |
| α-helix | 119-130 | 12 | |
| α-helix | 148-157 | 10 | |
| β-strand | 166-169 | 4 | 16 |
| α-helix | 179-194 | 16 | |
| β-strand | 198-203 | 6 | 16 |
| β-strand | 217 | 1 | 16 |
| β-strand | 219 | 1 | 18 |
| β-strand | 222 | 1 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-43 | 21 | |
| α-helix | 45-54 | 10 | |
| α-helix | 55-59 | 5 | |
| β-strand | 66 | 1 | 6 |
| α-helix | 80-84 | 5 | |
| β-strand | 96 | 1 | 7 |
| β-strand | 115-116 | 2 | 8 |
| β-strand | 147-148 | 2 | 9 |
| β-strand | 149 | 1 | 8 |
| β-strand | 150 | 1 | 9 |
| β-strand | 165-166 | 2 | 9 |
| β-strand | 187-192 | 6 | 9 |
| β-strand | 204-205 | 2 | 8 |
| β-strand | 224 | 1 | 7 |
| β-strand | 226 | 1 | 6 |
| α-helix | 254-257 | 4 | |
| α-helix | 264-271 | 8 | |
| α-helix | 278-283 | 6 | |
| α-helix | 285-291 | 7 | |
| α-helix | 293-296 | 4 | |
| α-helix | 299-307 | 9 | |
| α-helix | 312-342 | 31 | |
| α-helix | 345-351 | 7 | |
| α-helix | 379-394 | 16 | |
| α-helix | 396-401 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-7 | 2 | 10 |
| β-strand | 8-9 | 2 | 11 |
| β-strand | 31-32 | 2 | 10 |
| β-strand | 38-41 | 4 | 12 |
| α-helix | 48-56 | 9 | |
| β-strand | 65-66 | 2 | 11 |
| β-strand | 67-68 | 2 | 13 |
| β-strand | 71-72 | 2 | 13 |
| α-helix | 84-87 | 4 | |
| β-strand | 90-92 | 3 | 12 |
| α-helix | 104-108 | 5 | |
| α-helix | 110-114 | 5 | |
| α-helix | 119-130 | 12 | |
| α-helix | 136-138 | 3 | |
| α-helix | 153-159 | 7 | |
| β-strand | 166-169 | 4 | 12 |
| α-helix | 179-194 | 16 | |
| β-strand | 198-203 | 6 | 12 |
| β-strand | 217-218 | 2 | 12 |
| β-strand | 223-224 | 2 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lipoprotein-releasing ABC transporter permease subunit LolC | C | protein | 399 | Escherichia coli (strain K12) | P0ADC3 (AlphaFold model) |
| Lipoprotein-releasing system transmembrane protein LolE | E | protein | 414 | Escherichia coli (strain K12) | P75958 (AlphaFold model) |
| Lipoprotein-releasing system ATP-binding protein LolD | D, F | protein | 241 | Escherichia coli (strain K12) | P75957 (AlphaFold model) |
>7ARI_1 Lipoprotein-releasing ABC transporter permease subunit LolC (chains C) MYQPVALFIGLRYMRGRAADRFGRFVSWLSTIGITLGVMALVTVLSVMNGFERELQNNIL GLMPQAILSSEHGSLNPQQLPETAVKLDGVNRVAPITTGDVVLQSARSVAVGVMLGIDPA QKDPLTPYLVNVKQTDLEPGKYNVILGEQLASQLGVNRGDQIRVMVPSASQFTPMGRIPS QRLFNVIGTFAANSEVDGYEMLVNIEDASRLMRYPAGNITGWRLWLDEPLKVDSLSQQKL PEGSKWQDWRDRKGELFQAVRMEKNMMGLLLSLIVAVAAFNIITSLGLMVMEKQGEVAIL QTQGLTPRQIMMVFMVQGASAGIIGAILGAALGALLASQLNNLMPIIGVLLDGAALPVAI EPLQVIVIALVAMAIALLSTLYPSWRAAATQPAEALRYE
>7ARI_2 Lipoprotein-releasing system transmembrane protein LolE (chains E) MAMPLSLLIGLRFSRGRRRGGMVSLISVISTIGIALGVAVLIVGLSAMNGFERELNNRIL AVVPHGEIEAVDQPWTNWQEALDHVQKVPGIAAAAPYINFTGLVESGANLRAIQVKGVNP QQEQRLSALPSFVQGDAWRNFKAGEQQIIIGKGVADALKVKQGDWVSIMIPNSNPEHKLM QPKRVRLHVAGILQLSGQLDHSFAMIPLADAQQYLDMGSSVSGIALKMTDVFNANKLVRD AGEVTNSYVYIKSWIGTYGYMYRDIQMIRAIMYLAMVLVIGVACFNIVSTLVMAVKDKSG DIAVLRTLGAKDGLIRAIFVWYGLLAGLFGSLCGVIIGVVVSLQLTPIIEWIEKLIGHQF LSSDIYFIDFLPSELHWLDVFYVLVTALLLSLLASWYPARRASNIDPARVLSGQ
>7ARI_3 Lipoprotein-releasing system ATP-binding protein LolD (chains D, F) MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDT PTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPA EINSRALEMLKAVGLDHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAEHHHHHHH H
Structural basis for bacterial lipoprotein relocation by the transporter LolCDE. Tang, X., Chang, S., Zhang, K. et al. Nat Struct Mol Biol (2021) 28:347-355. DOI 10.1038/s41594-021-00573-x · PubMed
Other PDB entries of the same protein (UniProt P0ADC3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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