8OJG: MlaCD complex

Name: PDB 8OJG: Structure of the MlaCD complex (2:6 stoichiometry)
Published: 2024-07-10
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: lipid transport

Structure of the MlaCD complex (2:6 stoichiometry). Determined by electron microscopy at 4.38 Å resolution. Released 10 Jul 2024.

Method: Electron microscopy
Resolution: 4.38 Å
Organism: Escherichia coli
Chains: 8
Atoms: 8,348
Mol. weight: 165.54 kDa
Released: 10 Jul 2024

Explore 8OJG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8OJG contains 30 α-helices and 82 β-strands across 8 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: 1 helix, 7 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	1
β-strand	57-60	4	1
β-strand	63-72	10	1
β-strand	81-87	7	1
β-strand	98-103	6	1
β-strand	110-115	6	1
β-strand	133	1	1
α-helix	143-151	9

Chain B: 1 helix, 12 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	2
β-strand	57	1	3
β-strand	60	1	4
β-strand	63	1	4
β-strand	67	1	3
β-strand	68-73	6	2
β-strand	80-87	8	2
β-strand	94	1	5
β-strand	98-103	6	4
β-strand	110-115	6	4
β-strand	127	1	5
β-strand	133	1	2
α-helix	143-150	8

Chain C: 1 helix, 10 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	6
β-strand	58-60	3	7
β-strand	63	1	7
β-strand	68-73	6	6
β-strand	80-87	8	6
β-strand	94	1	8
β-strand	98-103	6	7
β-strand	110-115	6	7
β-strand	127	1	8
β-strand	133	1	6
α-helix	143-149	7

Chain D: 2 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	9
β-strand	57-60	4	9
β-strand	63-73	11	9
β-strand	80-87	8	9
β-strand	99-102	4	9
β-strand	111-114	4	9
α-helix	132-134	3
α-helix	143-150	8

Chain E: 1 helix, 12 β-strands

Element	Residues	Length	Sheet
β-strand	40-45	6	10
β-strand	57-59	3	11
β-strand	64-67	4	11
β-strand	68-73	6	10
β-strand	80-86	7	10
β-strand	94	1	12
β-strand	98-102	5	11
β-strand	111-115	5	11
β-strand	120	1	13
β-strand	124	1	13
β-strand	127	1	12
β-strand	133	1	10
α-helix	145-149	5

Chain F: 1 helix, 15 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	14
β-strand	57-58	2	15
β-strand	59	1	16
β-strand	60	1	15
β-strand	63-67	5	15
β-strand	68-73	6	14
β-strand	80-87	8	14
β-strand	94	1	17
β-strand	98	1	18
β-strand	103-104	2	19
β-strand	108-110	3	19
β-strand	113	1	16
β-strand	115	1	18
β-strand	127	1	17
β-strand	133	1	14
α-helix	145-148	4

Chain G: 11 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	27-44	18
α-helix	46-51	6
α-helix	56-59	4
α-helix	60-64	5
α-helix	65-67	3
α-helix	71-78	8
α-helix	87-109	23
β-strand	116-119	4	20
α-helix	120-122	3
β-strand	130-131	2	21
β-strand	134	1	22
β-strand	135-139	5	20
β-strand	143-146	4	20
β-strand	148	1	23
β-strand	149	1	22
β-strand	152-154	3	21
β-strand	161-163	3	21
β-strand	168	1	23
β-strand	171	1	23
α-helix	175-180	6
α-helix	183-188	6
α-helix	190-200	11

Chain H: 12 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	27-39	13
α-helix	42-45	4
α-helix	46-49	4
α-helix	56-63	8
α-helix	65-67	3
β-strand	68	1	24
α-helix	70-77	8
α-helix	87-104	18
α-helix	108-111	4
β-strand	116-119	4	25
α-helix	120-122	3
β-strand	130-132	3	24
β-strand	135-138	4	25
β-strand	148	1	26
β-strand	151-153	3	24
β-strand	162-163	2	24
β-strand	168	1	26
β-strand	171	1	26
α-helix	175-180	6
α-helix	183-188	6
α-helix	190-201	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Intermembrane phospholipid transport system binding protein MlaD	A, B, C, D, E, F	protein	183	Escherichia coli	P64604 (AlphaFold model)
Intermembrane phospholipid transport system binding protein MlaC	G, H	protein	211	Escherichia coli	P0ADV7 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>8OJG_1 Intermembrane phospholipid transport system binding protein MlaD (chains A, B, C, D, E, F)
MQTKKNEIWVGIFLLAALLAALFVCLKAANVTSIRTEPTYTLYATFDNIGGLKARSPVSI
GGVVVGRVADITLDPKTYLPRVTLEIEQRYNHIPDTSSLSIRTSGLLGEQYLALNVGFED
PELGTAILKDGDTIQDTKSAMVLEDLIGQFLYGSKGDDNKNSGDAPAAAPGNNETTEPVG
TTK

Sequence of entity 2 (G, H), FASTA

>8OJG_2 Intermembrane phospholipid transport system binding protein MlaC (chains G, H)
MFKRLMMVALLVIAPLSAATAADQTNPYKLMDEAAQKTFDRLKNEQPQIRANPDYLRTIV
DQELLPYVQVKYAGALVLGQYYKSATPAQREAYFAAFREYLKQAYGQALAMYHGQTYQIA
PEQPLGDKTIVPIRVTIIDPNGRPPVRLDFQWRKNSQTGNWQAYDMIAEGVSMITTKQNE
WGTLLRTKGIDGLTAQLKSISQQKITLEEKK

Primary citation

Structure of the MlaC-MlaD complex reveals molecular basis of periplasmic phospholipid transport. Wotherspoon, P., Johnston, H., Hardy, D.J. et al. Nat Commun (2024) 15:6394-6394. DOI 10.1038/s41467-024-50615-3 · PubMed

Other PDB entries of the same protein (UniProt P64604 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8HPZ 2.3 Å, Crystal structure of the MlaD domain of the MlaD protein from Escherichia coli (Form I)
8HQ9 2.7 Å, Crystal structure of the MlaD domain of the MlaD protein from Escherichia coli (Form II)
7CGE 2.9 Å, The overall structure of nucleotide free MlaFEDB complex
6XBD 3.05 Å, Cryo-EM structure of MlaFEDB in nanodiscs with phospholipid substrates
8HQA 3.2 Å, Crystal structure of the ectodomain of the MlaD protein from Escherichia coli in the…
6ZY3 3.3 Å, Cryo-EM structure of MlaFEDB in complex with phospholipid
6ZY9 3.3 Å, Cryo-EM structure of MlaFEDB in complex with AMP-PNP
6ZY2 3.6 Å, Cryo-EM structure of apo MlaFEDB
7CH0 3.7 Å, The overall structure of the MlaFEDB complex in ATP-bound EQclose conformation (Mutation…
6ZY4 4.1 Å, Cryo-EM structure of MlaFEDB in complex with ADP
7CGN 4.3 Å, The overall structure of the MlaFEDB complex in ATP-bound EQtall conformation (Mutation…
8OJ4 4.35 Å, Structure of the MlaCD complex (1:6 stoichiometry)

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