6XGZ: PDB entry 6XGZ

Crystal structure of E. coli MlaFB ABC transport subunits in the monomeric state. Determined by X-ray diffraction at 2.6 Å resolution. Released 15 Jul 2020.

Method: X-ray diffraction
Resolution: 2.6 Å
Organisms: Escherichia coli LAU-EC10, Escherichia coli
Chains: 8
Atoms: 11,433
Mol. weight: 166.87 kDa
Ligands: PO4
Released: 15 Jul 2020

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

Secondary structure: helices and β-sheets

6XGZ contains 67 α-helices and 65 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: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	7-18	12	1
β-strand	21-32	12	1
β-strand	36-40	5	2
α-helix	47-54	8
β-strand	62-67	6	1
β-strand	70-71	2	1
α-helix	77-84	8
β-strand	87-90	4	2
α-helix	102-113	12
α-helix	118-132	15
α-helix	135-137	3
α-helix	142-144	3
α-helix	147-158	12
β-strand	165-169	5	2
α-helix	177-194	18
β-strand	197-201	5	2
α-helix	205-209	5
β-strand	214-219	6	2
β-strand	222-226	5	2
α-helix	229-233	5
α-helix	238-245	8
α-helix	261-265	5

Chains B and D: 4 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	-2-1	4	3
β-strand	5-10	6	3
β-strand	13-20	8	3
α-helix	26-30	5
α-helix	32-35	4
β-strand	41-50	10	3
α-helix	52-67	16
β-strand	73-75	3	3
α-helix	79-87	9

Chain C: 12 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	7-18	12	4
β-strand	21-32	12	4
β-strand	36-40	5	5
α-helix	47-54	8
β-strand	62-67	6	4
β-strand	70-71	2	4
α-helix	77-84	8
β-strand	87-90	4	5
α-helix	102-113	12
α-helix	118-132	15
α-helix	135-137	3
α-helix	142-144	3
α-helix	147-158	12
β-strand	165-169	5	5
α-helix	177-194	18
β-strand	197-201	5	5
α-helix	205-209	5
β-strand	214-219	6	5
β-strand	222-227	6	5
α-helix	229-233	5
α-helix	238-247	10
α-helix	261-265	5

Chain E: 13 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	7-13	7	7
β-strand	14	1	8
β-strand	15	1	7
β-strand	17-18	2	9
β-strand	21-22	2	9
β-strand	27	1	8
β-strand	30-32	3	7
β-strand	36-40	5	10
α-helix	47-54	8
β-strand	62-67	6	7
β-strand	70-71	2	7
α-helix	77-83	7
α-helix	84-86	3
β-strand	87-90	4	10
α-helix	102-113	12
α-helix	118-132	15
α-helix	135-137	3
α-helix	142-144	3
α-helix	149-158	10
β-strand	165-169	5	10
α-helix	177-194	18
β-strand	197-201	5	10
α-helix	205-211	7
β-strand	214-219	6	10
β-strand	222-227	6	10
α-helix	229-234	6
α-helix	238-245	8
α-helix	261-265	5

Chain F: 4 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	-2-0	3	11
β-strand	5-10	6	11
β-strand	13-20	8	11
α-helix	26-30	5
α-helix	32-35	4
β-strand	41-50	10	11
α-helix	52-67	16
β-strand	73-75	3	11
α-helix	79-87	9

Chain G: 14 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	7-18	12	12
β-strand	21-32	12	12
β-strand	36-40	5	13
α-helix	47-54	8
β-strand	62-67	6	12
β-strand	70-71	2	12
α-helix	77-83	7
α-helix	84-86	3
β-strand	87-90	4	13
α-helix	102-113	12
α-helix	118-132	15
α-helix	135-137	3
α-helix	142-144	3
α-helix	147-158	12
β-strand	165-169	5	13
α-helix	177-194	18
β-strand	197-201	5	13
α-helix	205-211	7
β-strand	214-219	6	13
β-strand	222-227	6	13
α-helix	229-233	5
α-helix	238-247	10
α-helix	253-257	5
α-helix	261-265	5

Chain H: 4 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	-3-1	5	14
β-strand	5-10	6	14
β-strand	13-20	8	14
α-helix	26-30	5
α-helix	32-35	4
β-strand	41-50	10	14
α-helix	52-67	16
β-strand	73-75	3	14
α-helix	79-87	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Organic solvent ABC transporter ATP-binding protein	A, C, E, G	protein	269	Escherichia coli LAU-EC10	P63386 (AlphaFold model)
ABC transporter maintaining OM lipid asymmetry, cytoplasmic STAS component	B, D, F, H	protein	109	Escherichia coli	P64602 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>6XGZ_1 Organic solvent ABC transporter ATP-binding protein (chains A, C, E, G)
MEQSVANLVDMRDVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAP
DHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPL
LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM
GVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAWILADKKIVAHGSAQALQANPDPRV
RQFLDGIADGPVPFRYPAGDYHADLLPGS

Sequence of entity 2 (B, D, F, H), FASTA

>6XGZ_2 ABC transporter maintaining OM lipid asymmetry, cytoplasmic STAS component (chains B, D, F, H)
MHHHHHHENLYFQSESLSWMQTGDTLALSGELDQDVLLPLWEMREEAVKGITCIDLSRVS
RVDTGGLALLLHLIDLAKKQGNNVTLQGVNDKVYTLAKLYNLPADVLPR

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	8

Water and common crystallization additives (EDO, GOL) are not listed.

Primary citation

Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation. Kolich, L.R., Chang, Y.T., Coudray, N. et al. Elife (2020) 9. DOI 10.7554/eLife.60030 · PubMed

Other PDB entries of the same protein (UniProt P63386 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6XGY 2.9 Å, Crystal structure of E. coli MlaFB ABC transport subunits in the dimeric state
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
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
7CH6 3.4 Å, Cryo-EM structure of E.coli MlaFEB with AMPPNP
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…
7CH7 3.9 Å, Cryo-EM structure of E.coli MlaFEB
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…

Browse structure collections

About this viewer

MolViewer shows 6XGZ 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.