6F3Z: PDB entry 6F3Z

Complex of E. coli LolA and periplasmic domain of LolC. Determined by X-ray diffraction at 2.0 Å resolution. Released 25 Jul 2018.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Escherichia coli K-12
Chains: 4
Atoms: 6,688
Mol. weight: 97.12 kDa
Released: 25 Jul 2018

Explore 6F3Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6F3Z contains 40 α-helices and 50 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 A: 13 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	50-58	9
α-helix	60-62	3
β-strand	66-70	5	1
β-strand	75	1	2
α-helix	82-84	3
β-strand	90-96	7	1
β-strand	97-104	8	3
β-strand	109-117	9	3
α-helix	126-128	3
β-strand	129-130	2	3
α-helix	134-136	3
β-strand	143-147	5	3
α-helix	148-154	7
β-strand	161-173	13	3
β-strand	176-190	15	3
α-helix	195-198	4
β-strand	200-204	5	3
α-helix	205-211	7
α-helix	214-215	2
β-strand	219	1	2
β-strand	221-226	6	1
α-helix	229-231	3
α-helix	232-235	4
β-strand	244-248	5	1
α-helix	249-251	3
α-helix	254-276	23

Chains B and D: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	-4-10	15
β-strand	15-25	11	4
β-strand	31-42	12	4
β-strand	46-53	8	4
β-strand	57-62	6	4
β-strand	65-70	6	4
α-helix	71-73	3
β-strand	75-80	6	4
α-helix	81-83	3
α-helix	89-95	7
α-helix	98-101	4
β-strand	104-109	6	4
β-strand	112-117	6	4
β-strand	124-131	8	4
β-strand	137-144	8	4
β-strand	149-159	11	4
α-helix	164-167	4
α-helix	171-172	2
β-strand	176-179	4	4

Chain C: 13 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	50-58	9
α-helix	60-62	3
β-strand	66-70	5	5
β-strand	75	1	6
α-helix	82-84	3
β-strand	90-96	7	5
β-strand	97-104	8	7
β-strand	109-117	9	7
α-helix	126-128	3
β-strand	129-130	2	7
α-helix	134-136	3
β-strand	143-147	5	7
α-helix	148-154	7
β-strand	161-173	13	7
β-strand	176-190	15	7
α-helix	195-198	4
β-strand	200-204	5	7
α-helix	205-211	7
α-helix	214-215	2
β-strand	219	1	6
β-strand	221-226	6	5
α-helix	229-231	3
α-helix	232-235	4
α-helix	239-241	3
β-strand	244-248	5	5
α-helix	250-271	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Lipoprotein-releasing system transmembrane protein LolC	A, C	protein	230	Escherichia coli K-12	P0ADC3 (AlphaFold model)
Outer-membrane lipoprotein carrier protein	B, D	protein	206	Escherichia coli K-12	P61316 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6F3Z_1 Lipoprotein-releasing system transmembrane protein LolC (chains A, C)
MNGFERELQNNILGLMPQAILSSEHGSLNPQQLPETAVKLDGVNRVAPITTGDVVLQSAR
SVAVGVMLGIDPAQKDPLTPYLVNVKQTDLEPGKYNVILGEQLASQLGVNRGDQIRVMVP
SASQFTPMGRIPSQRLFNVIGTFAANSEVDGYEMLVNIEDASRLMRYPAGNITGWRLWLD
EPLKVDSLSQQKLPEGSKWQDWRDRKGELFQAVRMEKNMAAALEHHHHHH

Sequence of entity 2 (B, D), FASTA

>6F3Z_2 Outer-membrane lipoprotein carrier protein (chains B, D)
MGSSHHHHHHSSGLVPRGSHMASMDAASDLKSRLDKVSSFHASFTQKVTDGSGAAVQEGQ
GDLWVKRPNLFNWHMTQPDESILVSDGKTLWFYNPFVEQATATWLKDATGNTPFMLIARN
QSSDWQQYNIKQNGDDFVLTPKASNGNLKQFTINVGRDGTIHQFSAVEQDDQRSSYQLKS
QQNGAVDAAKFTFTPPQGVTVDDQRK

Primary citation

Insights into bacterial lipoprotein trafficking from a structure of LolA bound to the LolC periplasmic domain. Kaplan, E., Greene, N.P., Crow, A. et al. Proc Natl Acad Sci U S A (2018) 115:E7389-E7397. DOI 10.1073/pnas.1806822115 · 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
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
7ARL 3.2 Å, LolCDE in complex with lipoprotein and ADP

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