6GKI: E coli MlaC in Variously Loaded States

Structure of E coli MlaC in Variously Loaded States. Determined by X-ray diffraction at 2.23 Å resolution. Released 17 Apr 2019.

Method: X-ray diffraction
Resolution: 2.23 Å
Organism: Escherichia coli K-12
Chains: 2
Atoms: 3,132
Mol. weight: 46.55 kDa
Released: 17 Apr 2019

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

Secondary structure: helices and β-sheets

6GKI contains 28 α-helices and 12 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: 14 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	27-44	18
α-helix	46-51	6
α-helix	55-59	5
α-helix	60-64	5
α-helix	65-67	3
β-strand	68	1	1
α-helix	70-78	9
α-helix	79-81	3
α-helix	87-108	22
α-helix	109-111	3
β-strand	117-119	3	1
α-helix	120-122	3
β-strand	130-137	8	1
α-helix	138-139	2
α-helix	143-145	3
β-strand	146-154	9	1
β-strand	161-168	8	1
β-strand	171-172	2	1
α-helix	178-201	24
α-helix	204-205	2

Chain B: 14 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	27-44	18
α-helix	46-51	6
α-helix	55-59	5
α-helix	60-64	5
α-helix	65-67	3
β-strand	68	1	2
α-helix	70-78	9
α-helix	80-84	5
α-helix	87-109	23
β-strand	116-119	4	2
α-helix	120-122	3
β-strand	130-138	9	2
α-helix	139	1
α-helix	143-145	3
β-strand	146-155	10	2
β-strand	160-168	9	2
β-strand	171-172	2	2
α-helix	173-180	8
α-helix	182-201	20
α-helix	204-205	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Probable phospholipid-binding protein MlaC	A, B	protein	198	Escherichia coli K-12	P0ADV7 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6GKI_1 Probable phospholipid-binding protein MlaC (chains A, B)
ADQTNPYKLMDEAAQKTFDRLKNEQPQIRANPDYLRTIVDQELLPYVQVKYAGALVLGQY
YKSATPAQREAYFAAFREYLKQAYGQALAMYHGQTYQIAPEQPLGDKTIVPIRVTIIDPN
GRPPVRLDFQWRKNSQTGNWQAYDMIAEGVSMITTKQNEWGTLLRTKGIDGLTAQLKSIS
QQKITLEEKKLEHHHHHH

Primary citation

Evidence for phospholipid export from the bacterial inner membrane by the Mla ABC transport system. Hughes, G.W., Hall, S.C.L., Laxton, C.S. et al. Nat Microbiol (2019) 4:1692-1705. DOI 10.1038/s41564-019-0481-y · PubMed

Other PDB entries of the same protein (UniProt P0ADV7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5UWA 1.5 Å, Structure of E. coli phospholipid binding protein MlaC
7VR6 2.5 Å, Crystal structure of MlaC from Escherichia coli in quasi-open state
8I8X 3.25 Å, Cryo-EM Structure of OmpC3-MlaA-MlaC Complex in MSP2N2 Nanodiscs
8OJ4 4.35 Å, Structure of the MlaCD complex (1:6 stoichiometry)
8OJG 4.38 Å, Structure of the MlaCD complex (2:6 stoichiometry)

Browse structure collections

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