LolCDE in complex with lipoprotein and AMPPNP complex undimerized form. Determined by electron microscopy at 3.2 Å resolution. Released 7 Apr 2021.
Explore 7ARJ in 3D Show helices and sheets RCSB PDB PDBe
7ARJ contains 51 α-helices and 60 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 | 23-27 | 5 | |
| α-helix | 29-55 | 27 | |
| α-helix | 56-60 | 5 | |
| β-strand | 66-69 | 4 | 1 |
| β-strand | 75 | 1 | 2 |
| β-strand | 93-96 | 4 | 1 |
| β-strand | 98-104 | 7 | 3 |
| β-strand | 111-117 | 7 | 3 |
| β-strand | 129 | 1 | 3 |
| α-helix | 134-136 | 3 | |
| β-strand | 143-147 | 5 | 3 |
| α-helix | 148-152 | 5 | |
| β-strand | 161-166 | 6 | 3 |
| α-helix | 170-172 | 3 | |
| β-strand | 180-190 | 11 | 3 |
| β-strand | 202-204 | 3 | 3 |
| β-strand | 219 | 1 | 2 |
| β-strand | 221-224 | 4 | 1 |
| α-helix | 240-241 | 2 | |
| β-strand | 245-247 | 3 | 1 |
| α-helix | 249-251 | 3 | |
| α-helix | 256-270 | 15 | |
| α-helix | 273-292 | 20 | |
| α-helix | 295-303 | 9 | |
| α-helix | 307-311 | 5 | |
| α-helix | 313-317 | 5 | |
| α-helix | 320-338 | 19 | |
| α-helix | 362-378 | 17 | |
| α-helix | 381-388 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-7 | 2 | 16 |
| β-strand | 13-16 | 4 | 17 |
| β-strand | 21-25 | 5 | 17 |
| β-strand | 31-32 | 2 | 16 |
| β-strand | 38-41 | 4 | 18 |
| α-helix | 48-54 | 7 | |
| β-strand | 67-68 | 2 | 16 |
| α-helix | 84-87 | 4 | |
| β-strand | 89-91 | 3 | 18 |
| α-helix | 104-108 | 5 | |
| α-helix | 110-114 | 5 | |
| α-helix | 122-124 | 3 | |
| β-strand | 166-168 | 3 | 18 |
| α-helix | 181-183 | 3 | |
| α-helix | 190-192 | 3 | |
| β-strand | 199-203 | 5 | 18 |
| β-strand | 216-217 | 2 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-16 | 4 | |
| α-helix | 22-24 | 3 | |
| α-helix | 26-58 | 33 | |
| β-strand | 66-69 | 4 | 4 |
| β-strand | 75 | 1 | 5 |
| α-helix | 80-83 | 4 | |
| β-strand | 91-97 | 7 | 4 |
| β-strand | 98-99 | 2 | 6 |
| β-strand | 103-104 | 2 | 7 |
| β-strand | 112 | 1 | 7 |
| β-strand | 115-118 | 4 | 6 |
| α-helix | 123-125 | 3 | |
| α-helix | 129-131 | 3 | |
| β-strand | 133 | 1 | 8 |
| β-strand | 147-148 | 2 | 9 |
| β-strand | 149-150 | 2 | 6 |
| β-strand | 151 | 1 | 8 |
| α-helix | 152-158 | 7 | |
| β-strand | 165-166 | 2 | 9 |
| β-strand | 168-170 | 3 | 7 |
| α-helix | 181-182 | 2 | |
| β-strand | 183-184 | 2 | 7 |
| β-strand | 187-189 | 3 | 9 |
| β-strand | 193 | 1 | 8 |
| β-strand | 204-207 | 4 | 6 |
| α-helix | 208-214 | 7 | |
| β-strand | 221 | 1 | 5 |
| β-strand | 223-228 | 6 | 4 |
| α-helix | 240-242 | 3 | |
| β-strand | 250-252 | 3 | 4 |
| α-helix | 255-258 | 4 | |
| α-helix | 261-267 | 7 | |
| α-helix | 268-270 | 3 | |
| α-helix | 272-283 | 12 | |
| α-helix | 285-297 | 13 | |
| α-helix | 299-308 | 10 | |
| α-helix | 312-343 | 32 | |
| α-helix | 345-356 | 12 | |
| α-helix | 378-394 | 17 | |
| α-helix | 397-401 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-7 | 2 | 10 |
| β-strand | 9 | 1 | 11 |
| β-strand | 16 | 1 | 12 |
| β-strand | 21 | 1 | 12 |
| β-strand | 31-32 | 2 | 10 |
| β-strand | 37-38 | 2 | 13 |
| β-strand | 41 | 1 | 14 |
| α-helix | 48-54 | 7 | |
| β-strand | 65 | 1 | 11 |
| β-strand | 68 | 1 | 10 |
| β-strand | 71 | 1 | 10 |
| α-helix | 78-87 | 10 | |
| β-strand | 89-92 | 4 | 13 |
| α-helix | 104-108 | 5 | |
| α-helix | 110-114 | 5 | |
| α-helix | 122-133 | 12 | |
| α-helix | 148-159 | 12 | |
| β-strand | 166-170 | 5 | 13 |
| α-helix | 178-183 | 6 | |
| α-helix | 185-190 | 6 | |
| β-strand | 199-202 | 4 | 13 |
| β-strand | 214 | 1 | 13 |
| β-strand | 217 | 1 | 14 |
| β-strand | 219 | 1 | 15 |
| β-strand | 222 | 1 | 15 |
| 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) |
| LPP | V | protein | 10 | Escherichia coli K-12 | P69776 (AlphaFold model) |
>7ARJ_1 Lipoprotein-releasing ABC transporter permease subunit LolC (chains C) MYQPVALFIGLRYMRGRAADRFGRFVSWLSTIGITLGVMALVTVLSVMNGFERELQNNIL GLMPQAILSSEHGSLNPQQLPETAVKLDGVNRVAPITTGDVVLQSARSVAVGVMLGIDPA QKDPLTPYLVNVKQTDLEPGKYNVILGEQLASQLGVNRGDQIRVMVPSASQFTPMGRIPS QRLFNVIGTFAANSEVDGYEMLVNIEDASRLMRYPAGNITGWRLWLDEPLKVDSLSQQKL PEGSKWQDWRDRKGELFQAVRMEKNMMGLLLSLIVAVAAFNIITSLGLMVMEKQGEVAIL QTQGLTPRQIMMVFMVQGASAGIIGAILGAALGALLASQLNNLMPIIGVLLDGAALPVAI EPLQVIVIALVAMAIALLSTLYPSWRAAATQPAEALRYE
>7ARJ_2 Lipoprotein-releasing system transmembrane protein LolE (chains E) MAMPLSLLIGLRFSRGRRRGGMVSLISVISTIGIALGVAVLIVGLSAMNGFERELNNRIL AVVPHGEIEAVDQPWTNWQEALDHVQKVPGIAAAAPYINFTGLVESGANLRAIQVKGVNP QQEQRLSALPSFVQGDAWRNFKAGEQQIIIGKGVADALKVKQGDWVSIMIPNSNPEHKLM QPKRVRLHVAGILQLSGQLDHSFAMIPLADAQQYLDMGSSVSGIALKMTDVFNANKLVRD AGEVTNSYVYIKSWIGTYGYMYRDIQMIRAIMYLAMVLVIGVACFNIVSTLVMAVKDKSG DIAVLRTLGAKDGLIRAIFVWYGLLAGLFGSLCGVIIGVVVSLQLTPIIEWIEKLIGHQF LSSDIYFIDFLPSELHWLDVFYVLVTALLLSLLASWYPARRASNIDPARVLSGQ
>7ARJ_3 Lipoprotein-releasing system ATP-binding protein LolD (chains D, F) MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDT PTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPA EINSRALEMLKAVGLDHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAEHHHHHHH H
>7ARJ_4 LPP (chains V) CSSNAKIDQL
| ID | Name | Formula | Copies |
|---|---|---|---|
| PLM | Palmitic acid | C16 H32 O2 | 1 |
| Z41 | (2S)-3-hydroxypropane-1,2-diyl dihexadecanoate | C35 H68 O5 | 1 |
| MG | Magnesium ion | Mg | 2 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
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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