5NAA: PDB entry 5NAA

Lipoprotein-releasing system transmembrane protein LolC. Determined by X-ray diffraction at 1.88 Å resolution. Released 15 Nov 2017.

Method: X-ray diffraction
Resolution: 1.88 Å
Organism: Escherichia coli
Chains: 2
Atoms: 3,712
Mol. weight: 51.34 kDa
Released: 15 Nov 2017

Explore 5NAA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NAA contains 26 α-helices and 26 β-strands across 2 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	51-58	8
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	161-171	11	3
β-strand	178-190	13	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	254-270	17

Chain B: 13 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	51-54	4
α-helix	55-59	5
β-strand	66-70	5	4
β-strand	75	1	5
α-helix	82-84	3
β-strand	90-96	7	4
β-strand	97-104	8	6
β-strand	109-117	9	6
α-helix	126-128	3
β-strand	129-130	2	6
α-helix	134-136	3
β-strand	143-147	5	6
α-helix	148-154	7
β-strand	161-171	11	6
β-strand	178-190	13	6
α-helix	195-198	4
β-strand	200-204	5	6
α-helix	205-211	7
α-helix	214-215	2
β-strand	219	1	5
β-strand	221-226	6	4
α-helix	229-231	3
α-helix	232-235	4
β-strand	244-248	5	4
α-helix	249-251	3
α-helix	254-263	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Lipoprotein-releasing system transmembrane protein LolC	A, B	protein	230	Escherichia coli	P0ADC3 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5NAA_1 Lipoprotein-releasing system transmembrane protein LolC (chains A, B)
MNGFERELQNNILGLMPQAILSSEHGSLNPQQLPETAVKLDGVNRVAPITTGDVVLQSAR
SVAVGVMLGIDPAQKDPLTPYLVNVKQTDLEPGKYNVILGEQLASQLGVNRGDQIRVMVP
SASQFTPMGRIPSQRLFNVIGTFAANSEVDGYEMLVNIEDASRLMRYPAGNITGWRLWLD
EPLKVDSLSQQKLPEGSKWQDWRDRKGELFQAVRMEKNMAAALEHHHHHH

Primary citation

Structure and mechanotransmission mechanism of the MacB ABC transporter superfamily. Crow, A., Greene, N.P., Kaplan, E. et al. Proc Natl Acad Sci U S A (2017) 114:12572-12577. DOI 10.1073/pnas.1712153114 · PubMed

Other PDB entries of the same protein (UniProt P0ADC3 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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
7ARL 3.2 Å, LolCDE in complex with lipoprotein and ADP

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