4JBW: E. coli maltose transporter MalFGK2

Crystal structure of E. coli maltose transporter MalFGK2 in complex with its regulatory protein EIIAglc. Determined by X-ray diffraction at 3.91 Å resolution. Released 12 Jun 2013.

Method: X-ray diffraction
Resolution: 3.91 Å
Organism: Escherichia coli
Chains: 12
Atoms: 27,958
Mol. weight: 423.02 kDa
Ligands: PGV
Released: 12 Jun 2013

Explore 4JBW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4JBW contains 184 α-helices and 228 β-strands across 12 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: 17 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	10
β-strand	16-25	10	10
β-strand	31-35	5	11
α-helix	42-50	9
β-strand	57-62	6	10
β-strand	66	1	10
α-helix	73-75	3
β-strand	77-80	4	11
α-helix	92-96	5
α-helix	98-101	4
α-helix	107-120	14
α-helix	124-126	3
α-helix	131-133	3
α-helix	136-150	15
β-strand	154-158	5	11
α-helix	166-171	6
α-helix	173-183	11
β-strand	186-191	6	11
α-helix	194-200	7
β-strand	203-208	6	11
β-strand	211-216	6	11
α-helix	218-223	6
β-strand	227	1	12
α-helix	228-233	6
α-helix	238-239	2
β-strand	240-242	3	13
β-strand	245-249	5	14
β-strand	254-257	4	14
β-strand	265-268	4	14
β-strand	270	1	15
β-strand	282-285	4	13
α-helix	287-289	3
α-helix	290	1
β-strand	291-292	2	16
β-strand	299-300	2	16
β-strand	303-309	7	17
β-strand	313-319	7	17
β-strand	326-332	7	17
β-strand	342	1	17
β-strand	345-346	2	16
β-strand	353-355	3	13
β-strand	360	1	12
β-strand	361-362	2	13
α-helix	363	1
β-strand	364	1	15

Chain B: 17 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	18
β-strand	16-25	10	18
β-strand	31-35	5	19
α-helix	42-50	9
β-strand	57-62	6	18
β-strand	66	1	18
α-helix	73-75	3
β-strand	77-80	4	19
α-helix	92-96	5
α-helix	98-101	4
α-helix	107-121	15
α-helix	124-126	3
α-helix	131-133	3
α-helix	136-150	15
β-strand	154-158	5	19
α-helix	166-183	18
β-strand	187-191	5	19
α-helix	194-200	7
β-strand	203-208	6	19
β-strand	211-216	6	19
α-helix	218-223	6
β-strand	227	1	20
α-helix	228-233	6
α-helix	238-239	2
β-strand	240-249	10	21
β-strand	254-257	4	21
β-strand	265-268	4	21
β-strand	270	1	22
β-strand	280-285	6	21
α-helix	287-289	3
α-helix	290	1
β-strand	291-292	2	23
β-strand	299-300	2	23
β-strand	303-309	7	24
β-strand	313-319	7	24
β-strand	326-332	7	24
β-strand	342	1	24
β-strand	345-346	2	23
α-helix	349-351	3
β-strand	352-355	4	21
β-strand	360	1	20
β-strand	361	1	21
α-helix	362-363	2
β-strand	364	1	22

Chain C: 17 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	42
β-strand	16-25	10	42
β-strand	31-35	5	43
α-helix	42-50	9
β-strand	57-62	6	42
β-strand	66	1	42
α-helix	73-75	3
β-strand	77-80	4	43
α-helix	92-96	5
α-helix	98-102	5
α-helix	107-120	14
α-helix	124-126	3
α-helix	131-133	3
α-helix	136-150	15
β-strand	154-158	5	43
α-helix	166-171	6
α-helix	173-183	11
β-strand	186-191	6	43
α-helix	194-200	7
β-strand	203-208	6	43
β-strand	211-216	6	43
α-helix	218-223	6
β-strand	227	1	44
α-helix	228-233	6
α-helix	238-239	2
β-strand	240-242	3	45
β-strand	245-249	5	46
β-strand	254-257	4	46
β-strand	265-268	4	46
β-strand	270	1	47
β-strand	282-285	4	45
α-helix	287-289	3
α-helix	290	1
β-strand	291-292	2	48
β-strand	299-300	2	48
β-strand	303-309	7	49
β-strand	313-319	7	49
β-strand	326-332	7	49
β-strand	342	1	49
β-strand	345-346	2	48
β-strand	352-355	4	45
β-strand	360	1	44
β-strand	361	1	45
α-helix	362-363	2
β-strand	364	1	47

Chain D: 16 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	50
β-strand	16-25	10	50
β-strand	31-35	5	51
α-helix	42-50	9
β-strand	57-62	6	50
β-strand	66	1	50
α-helix	73-75	3
β-strand	77-80	4	51
α-helix	92-101	10
α-helix	107-120	14
α-helix	124-126	3
α-helix	131-133	3
α-helix	136-150	15
β-strand	154-158	5	51
α-helix	166-183	18
β-strand	186-191	6	51
α-helix	194-200	7
β-strand	203-208	6	51
β-strand	211-216	6	51
α-helix	218-223	6
β-strand	227	1	52
α-helix	228-233	6
α-helix	238-239	2
β-strand	240-243	4	53
β-strand	245-249	5	54
β-strand	254-257	4	54
β-strand	265-268	4	54
β-strand	270	1	55
β-strand	282-285	4	53
α-helix	287-289	3
α-helix	290	1
β-strand	291-292	2	56
β-strand	299-300	2	56
β-strand	303-309	7	57
β-strand	313-319	7	57
β-strand	326-332	7	57
β-strand	342	1	57
β-strand	345-346	2	56
α-helix	349-351	3
β-strand	353-355	3	53
β-strand	360	1	52
β-strand	361	1	53
α-helix	362-363	2
β-strand	364	1	55

Chain F: 28 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	20-35	16
α-helix	40-43	4
α-helix	45-58	14
α-helix	65-78	14
α-helix	80-89	10
β-strand	92	1	1
β-strand	95	1	2
β-strand	100	1	3
α-helix	102-104	3
α-helix	109-111	3
β-strand	113-115	3	4
β-strand	120-124	5	4
β-strand	127	1	5
β-strand	130	1	5
β-strand	131-137	7	4
β-strand	143-149	7	4
β-strand	155	1	6
α-helix	157	1
β-strand	158	1	4
α-helix	159	1
β-strand	160-161	2	4
α-helix	165-166	2
α-helix	169-171	3
α-helix	173-178	6
α-helix	180-184	5
β-strand	186	1	6
β-strand	187-189	3	4
β-strand	195-198	4	4
β-strand	203-209	7	4
β-strand	211-213	3	7
β-strand	219-221	3	7
β-strand	227-231	5	7
β-strand	236-239	4	7
β-strand	250-251	2	7
β-strand	255	1	3
β-strand	258	1	1
α-helix	262-268	7
α-helix	271-306	36
α-helix	314-326	13
α-helix	329-339	11
α-helix	347-351	5
α-helix	365-392	28
α-helix	397-405	9
α-helix	410-413	4
α-helix	414-418	5
α-helix	419-438	20
α-helix	441-447	7
β-strand	453	1	8
α-helix	454	1
β-strand	462	1	8
α-helix	467-476	10
β-strand	483	1	2
α-helix	484-499	16
α-helix	502-506	5

Chain G: 18 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	10-39	30
α-helix	57-61	5
α-helix	75-77	3
α-helix	81-111	31
α-helix	117-130	14
α-helix	137-150	14
α-helix	152-154	3
α-helix	159-166	8
α-helix	171-181	11
α-helix	187-195	9
α-helix	199-202	4
α-helix	203-207	5
α-helix	208-210	3
α-helix	212-228	17
α-helix	231-236	6
α-helix	240-242	3
α-helix	245-248	4
β-strand	253	1	9
β-strand	258	1	9
α-helix	263-282	20

Chain H: 28 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	20-23	4
α-helix	26-35	10
α-helix	40-43	4
α-helix	45-58	14
α-helix	65-78	14
α-helix	80-88	9
β-strand	100	1	32
α-helix	102-109	8
β-strand	120-122	3	33
β-strand	127	1	34
β-strand	130	1	34
β-strand	131	1	35
β-strand	135-136	2	33
β-strand	143	1	33
β-strand	144-145	2	36
β-strand	149	1	35
α-helix	157	1
β-strand	158	1	33
α-helix	159	1
β-strand	160-161	2	36
α-helix	165-166	2
α-helix	169-171	3
α-helix	173-178	6
α-helix	180-184	5
β-strand	187-189	3	33
β-strand	195-198	4	33
β-strand	203-205	3	33
β-strand	211	1	37
β-strand	219-220	2	38
β-strand	221	1	37
β-strand	227-228	2	38
β-strand	229-231	3	39
β-strand	236-238	3	39
β-strand	255	1	32
α-helix	262-267	6
α-helix	274-306	33
α-helix	314-326	13
α-helix	329-339	11
α-helix	347-351	5
α-helix	365-392	28
α-helix	397-405	9
α-helix	410-413	4
α-helix	414-418	5
α-helix	419-438	20
α-helix	441-447	7
β-strand	453	1	40
α-helix	454	1
β-strand	462	1	40
α-helix	467-476	10
α-helix	484-499	16
α-helix	502-507	6

Chain I: 23 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	6-8	3
α-helix	10-39	30
α-helix	57-61	5
α-helix	75-77	3
α-helix	81-112	32
α-helix	117-130	14
α-helix	137-150	14
α-helix	152-154	3
α-helix	159-166	8
α-helix	171-181	11
α-helix	187-195	9
α-helix	199-202	4
α-helix	203-207	5
α-helix	208-210	3
α-helix	212-228	17
α-helix	231-236	6
α-helix	240-242	3
α-helix	245-248	4
α-helix	249-251	3
β-strand	253	1	41
β-strand	258	1	41
α-helix	262-264	3
α-helix	265	1
α-helix	266-271	6
α-helix	272-282	11

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltose transport system permease protein MalF	F, H	protein	514	Escherichia coli	P02916 (AlphaFold model)
Maltose transport system permease protein MalG	G, I	protein	296	Escherichia coli	P68183 (AlphaFold model)
Maltose/maltodextrin import ATP-binding protein MalK	A, B, C, D	protein	381	Escherichia coli	P68187 (AlphaFold model)
Glucose-specific phosphotransferase enzyme IIA component	M, N, O, P	protein	172	Escherichia coli	P69783 (AlphaFold model)

Sequence of entity 1 (F, H), FASTA

>4JBW_1 Maltose transport system permease protein MalF (chains F, H)
MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANR
KAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTY
NFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNR
QALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSI
TADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGM
VLACLVQWEALRGKAVYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGVKPA
WFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFFKITLP
LLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVNYTYRIAFEGGG
GQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD

Sequence of entity 2 (G, I), FASTA

>4JBW_2 Maltose transport system permease protein MalG (chains G, I)
MAMVQPKSQKARLFITHLLLLLFIAAIMFPLLMVVAISLRQGNFATGSLIPEQISWDHWK
LALGFSVEQADGRITPPPFPVLLWLWNSVKVAGISAIGIVALSTTCAYAFARMRFPGKAT
LLKGMLIFQMFPAVLSLVALYALFDRLGEYIPFIGLNTHGGVIFAYLGGIALHVWTIKGY
FETIDSSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDV
NSYTLAVGMQQYLNPQNYLWGDFAAAAVMSALPITIVFLLAQRWLVNGLTAGGVKG

Sequence of entity 3 (A, B, C, D), FASTA

>4JBW_3 Maltose/maltodextrin import ATP-binding protein MalK (chains A, B, C, D)
MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL
FIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEV
LQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLH
KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMN
FLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVIL
EGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGT
ACRRLHKEPGVASASHHHHHH

Sequence of entity 4 (M, N, O, P), FASTA

>4JBW_4 Glucose-specific phosphotransferase enzyme IIA component (chains M, N, O, P)
SNAMGLFDKLKSLVSDDKKDTGTIEIIAPLSGEIVNIEDVPDVVFAEKIVGDGIAIKPTG
NKMVAPVDGTIGKIFETNHAFSIESDSGVELFVHFGIDTVELKGEGFKRIAEEGQRVKVG
DTVIEFDLPLLEEKAKSTLTPVVISNMDEIKELIKLSGSVTVGETPVIRIKK

Ligands and cofactors

ID	Name	Formula	Copies
PGV	(1R)-2-{[{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(palmitoylo…	C40 H77 O10 P	2

Primary citation

Carbon catabolite repression of the maltose transporter revealed by X-ray crystallography. Chen, S., Oldham, M.L., Davidson, A.L. et al. Nature (2013) 499:364-368. DOI 10.1038/nature12232 · PubMed

Other PDB entries of the same protein (UniProt P02916 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3RLF 2.2 Å, Crystal structure of the maltose-binding protein/maltose transporter complex in an…
3PUW 2.3 Å, Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-AlF4
3PUX 2.3 Å, Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-BeF3
4KI0 2.38 Å, Crystal structure of the maltose-binding protein/maltose transporter complex in an…
3PUV 2.4 Å, Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-VO4
2R6G 2.8 Å, The Crystal Structure of the E. coli Maltose Transporter
3PUZ 2.9 Å, Crystal Structure of a pre-translocation state MBP-Maltose transporter complex bound to…
4KHZ 2.9 Å, Crystal structure of the maltose-binding protein/maltose transporter complex in an…
3PUY 3.1 Å, Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to AMP-PNP…
3PV0 3.1 Å, Crystal Structure of a pre-translocation state MBP-Maltose transporter complex without…
9BCR 3.26 Å, Cryo-EM structure of a bacterial prototype ATP-binding cassette transporter MalFGK2.
9NQJ 3.34 Å, Cryo-EM structure of a bacterial prototype ATP-binding cassette transporter MalFGK2.

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