7V8I: LolCD(E171Q)E with bound AMPPNP in nanodiscs

LolCD(E171Q)E with bound AMPPNP in nanodiscs. Determined by electron microscopy at 3.6 Å resolution. Released 31 Aug 2022.

Method: Electron microscopy
Resolution: 3.6 Å
Organism: Escherichia coli K-12
Chains: 4
Atoms: 9,388
Mol. weight: 140.68 kDa
Ligands: ANP, MG
Released: 31 Aug 2022

Explore 7V8I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7V8I contains 50 α-helices and 41 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.

Chain C: 15 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	8-15	8
α-helix	23-27	5
α-helix	29-54	26
α-helix	55-59	5
β-strand	66-69	4	1
α-helix	77-79	3
β-strand	90-96	7	1
β-strand	97-104	8	2
β-strand	109-117	9	2
β-strand	129-130	2	3
β-strand	143	1	2
β-strand	145	1	2
β-strand	147	1	3
α-helix	149-154	6
β-strand	161-173	13	2
β-strand	176-185	10	2
β-strand	189-190	2	3
α-helix	196-198	3
β-strand	200-204	5	2
α-helix	205-211	7
β-strand	221-226	6	1
α-helix	234-236	3
β-strand	245-248	4	1
α-helix	255-292	38
α-helix	294-302	9
α-helix	307-334	28
α-helix	341-343	3
α-helix	362-378	17
α-helix	382-389	8

Chain D: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6-13	8	4
β-strand	25-32	8	4
β-strand	38-41	4	5
α-helix	49-55	7
β-strand	63-68	6	4
β-strand	71-72	2	4
α-helix	78-87	10
β-strand	89-92	4	5
α-helix	104-114	11
α-helix	119-133	15
α-helix	143-145	3
α-helix	148-160	13
β-strand	166-170	5	5
α-helix	178-194	17
β-strand	198-202	5	5
α-helix	206-210	5
β-strand	214-219	6	5
β-strand	222-227	6	5

Chain E: 18 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	12-16	5
α-helix	28-59	32
α-helix	78-86	9
β-strand	91-97	7	6
β-strand	98-106	9	7
β-strand	109-117	9	7
α-helix	123-126	4
α-helix	129-132	4
α-helix	138-141	4
β-strand	147	1	8
α-helix	152-158	7
β-strand	165-169	5	8
β-strand	184-188	5	8
α-helix	198-200	3
α-helix	208-214	7
β-strand	223-228	6	6
α-helix	234-242	9
α-helix	259-289	31
α-helix	290-294	5
α-helix	297-304	8
α-helix	314-343	30
α-helix	349-352	4
α-helix	353-355	3
α-helix	377-404	28
α-helix	407-409	3

Chain F: 9 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	6-15	10	9
β-strand	22-32	11	9
α-helix	33	1
β-strand	37-41	5	10
α-helix	49-55	7
β-strand	63-68	6	9
β-strand	71-72	2	9
α-helix	78-87	10
β-strand	89-92	4	10
α-helix	104-114	11
α-helix	119-133	15
α-helix	143-145	3
α-helix	148-161	14
β-strand	166-170	5	10
α-helix	178-194	17
β-strand	198-202	5	10
α-helix	206-210	5
β-strand	214-219	6	10
β-strand	222-226	5	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
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)
Lipoprotein-releasing system transmembrane protein LolE	E	protein	414	Escherichia coli K-12	P75958 (AlphaFold model)

Sequence of entity 1 (C), FASTA

>7V8I_1 Lipoprotein-releasing system transmembrane protein LolC (chains C)
MYQPVALFIGLRYMRGRAADRFGRFVSWLSTIGITLGVMALVTVLSVMNGFERELQNNIL
GLMPQAILSSEHGSLNPQQLPETAVKLDGVNRVAPITTGDVVLQSARSVAVGVMLGIDPA
QKDPLTPYLVNVKQTDLEPGKYNVILGEQLASQLGVNRGDQIRVMVPSASQFTPMGRIPS
QRLFNVIGTFAANSEVDGYEMLVNIEDASRLMRYPAGNITGWRLWLDEPLKVDSLSQQKL
PEGSKWQDWRDRKGELFQAVRMEKNMMGLLLSLIVAVAAFNIITSLGLMVMEKQGEVAIL
QTQGLTPRQIMMVFMVQGASAGIIGAILGAALGALLASQLNNLMPIIGVLLDGAALPVAI
EPLQVIVIALVAMAIALLSTLYPSWRAAATQPAEALRYE

Sequence of entity 2 (D, F), FASTA

>7V8I_2 Lipoprotein-releasing system ATP-binding protein LolD (chains D, F)
MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSVGEGEMMAIVGSSGSGKSTLLHLLGGLDT
PTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPA
EINSRALEMLKAVGLDHRANHRPSELSGGERQRVAIARALVNNPRLVLADQPTGNLDARN
ADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSLMGAE

Sequence of entity 3 (E), FASTA

>7V8I_3 Lipoprotein-releasing system transmembrane protein LolE (chains E)
MAMPLSLLIGLRFSRGRRRGGMVSLISVISTIGIALGVAVLIVGLSAMNGFERELNNRIL
AVVPHGEIEAVDQPWTNWQEALDHVQKVPGIAAAAPYINFTGLVESGANLRAIQVKGVNP
QQEQRLSALPSFVQGDAWRNFKAGEQQIIIGKGVADALKVKQGDWVSIMIPNSNPEHKLM
QPKRVRLHVAGILQLSGQLDHSFAMIPLADAQQYLDMGSSVSGIALKMTDVFNANKLVRD
AGEVTNSYVYIKSWIGTYGYMYRDIQMIRAIMYLAMVLVIGVACFNIVSTLVMAVKDKSG
DIAVLRTLGAKDGLIRAIFVWYGLLAGLFGSLCGVIIGVVVSLQLTPIIEWIEKLIGHQF
LSSDIYFIDFLPSELHWLDVFYVLVTALLLSLLASWYPARRASNIDPARVLSGQ

Ligands and cofactors

ID	Name	Formula	Copies
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	2
MG	Magnesium ion	Mg	2

Primary citation

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 P0ADC3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5NAA 1.88 Å, Lipoprotein-releasing system transmembrane protein LolC
6F3Z 2.0 Å, Complex of E. coli LolA and periplasmic domain of LolC
6F49 2.02 Å, Periplasmic domain of LolC lacking the Hook.
9RLC 2.8 Å, LolCDE complex with Lpp lipoprotein
9XRO 2.88 Å, LolCDE in complex with SMT-738_3
9RLJ 2.9 Å, LolCDE with bound ATPgammaS
9RLD 3.0 Å, LolCDE complex with Lpp lipoprotein
9RLG 3.09 Å, LolCDE complex with LolB lipoprotein
9RLF 3.17 Å, LolCDE complex with Pal lipoprotein
9RLE 3.18 Å, LolCDE complex with Pal lipoprotein
9RLH 3.19 Å, LolCDE complex with del 9-15 LolB lipoprotein
7ARJ 3.2 Å, LolCDE in complex with lipoprotein and AMPPNP complex undimerized form

Browse structure collections

About this viewer

MolViewer shows 7V8I directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.