4KI0: ABC transporter related protein

Crystal structure of the maltose-binding protein/maltose transporter complex in an outward-facing conformation bound to maltohexaose. Determined by X-ray diffraction at 2.38 Å resolution. Released 23 Oct 2013.

Method: X-ray diffraction
Resolution: 2.38 Å
Organism: Escherichia coli
Chains: 5
Atoms: 15,618
Mol. weight: 224.25 kDa
Ligands: UMQ, PGV, ANP, MG
Released: 23 Oct 2013

Explore 4KI0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4KI0 contains 97 α-helices and 99 β-strands across 5 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: 15 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	1
β-strand	16-26	11	1
β-strand	31-35	5	2
α-helix	42-50	9
β-strand	57-62	6	1
β-strand	65-66	2	1
α-helix	72-74	3
β-strand	77-80	4	2
α-helix	92-102	11
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	2
α-helix	166-183	18
β-strand	186-190	5	2
α-helix	194-200	7
β-strand	203-208	6	2
β-strand	211-216	6	2
α-helix	218-223	6
β-strand	227	1	3
α-helix	228-233	6
α-helix	238-239	2
β-strand	240-250	11	4
β-strand	253-257	5	4
β-strand	265-268	4	4
β-strand	270	1	5
β-strand	280-285	6	4
β-strand	291-292	2	6
β-strand	299-309	11	6
β-strand	313-319	7	6
α-helix	326	1
β-strand	327-332	6	6
β-strand	342-346	5	6
α-helix	349-351	3
β-strand	353-355	3	4
β-strand	360	1	3
β-strand	361-362	2	4
β-strand	364	1	5
α-helix	367-368	2

Chain B: 16 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	7
β-strand	17-26	10	7
α-helix	27	1
β-strand	31-35	5	8
α-helix	42-50	9
β-strand	57-62	6	7
β-strand	66	1	7
α-helix	72-74	3
β-strand	77-80	4	8
α-helix	92-104	13
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	8
α-helix	166-183	18
β-strand	186-190	5	8
α-helix	194-200	7
β-strand	203-208	6	8
β-strand	211-216	6	8
α-helix	218-223	6
β-strand	227	1	9
α-helix	228-233	6
α-helix	238-239	2
β-strand	240-250	11	10
β-strand	253-257	5	10
β-strand	265-268	4	10
β-strand	270	1	11
β-strand	280-285	6	10
β-strand	291-292	2	12
β-strand	299-309	11	12
β-strand	313-319	7	12
α-helix	326	1
β-strand	327-332	6	12
β-strand	342-346	5	12
α-helix	349-351	3
β-strand	353-355	3	10
β-strand	360	1	9
β-strand	361	1	10
β-strand	364	1	11
α-helix	367-368	2

Chain E: 22 helices, 24 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	7-10	4	13
α-helix	17-31	15
β-strand	35-38	4	13
α-helix	43-51	9
β-strand	59-63	5	13
α-helix	65-73	9
β-strand	76	1	14
α-helix	77-79	3
α-helix	83-87	5
β-strand	89	1	15
α-helix	91-95	5
β-strand	98-99	2	16
β-strand	102-103	2	16
β-strand	106-111	6	13
β-strand	114-118	5	17
β-strand	128	1	18
α-helix	132-140	9
β-strand	145-147	3	17
α-helix	154-162	9
β-strand	167-171	5	19
β-strand	176-182	7	19
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-227	6	17
α-helix	229-231	3
α-helix	232-238	7
β-strand	242-245	4	17
α-helix	246-248	3
β-strand	249	1	18
β-strand	250	1	20
β-strand	253	1	20
β-strand	258-259	2	21
β-strand	260-266	7	13
β-strand	267	1	14
α-helix	273-278	6
α-helix	279-284	6
α-helix	287-296	10
β-strand	301-302	2	13
β-strand	304	1	15
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	21
α-helix	330-331	2
α-helix	336-351	16
α-helix	357-369	13

Chain F: 26 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	15-35	21
α-helix	40-58	19
α-helix	60-62	3
α-helix	63-75	13
α-helix	76-80	5
α-helix	81-90	10
β-strand	92	1	22
β-strand	100	1	23
α-helix	102-111	10
β-strand	113-127	15	24
β-strand	130-137	8	24
β-strand	142-146	5	24
β-strand	149	1	24
β-strand	155-162	8	24
α-helix	169-171	3
α-helix	173-178	6
α-helix	180-184	5
β-strand	186-189	4	24
β-strand	195-198	4	24
β-strand	203-209	7	24
β-strand	211-213	3	25
β-strand	219-221	3	25
β-strand	227-231	5	25
β-strand	236-239	4	25
β-strand	250	1	25
β-strand	255	1	23
β-strand	258	1	22
α-helix	262-269	8
α-helix	271-274	4
α-helix	277-305	29
α-helix	314-326	13
α-helix	329-339	11
α-helix	346-354	9
α-helix	365-391	27
α-helix	392-394	3
α-helix	398-405	8
α-helix	410-413	4
α-helix	414-418	5
α-helix	419-438	20
α-helix	441-447	7
α-helix	451	1
β-strand	453	1	26
β-strand	462	1	26
α-helix	467-476	10
α-helix	484-504	21

Chain G: 18 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	9-39	31
β-strand	40	1	27
β-strand	54	1	27
α-helix	57-63	7
β-strand	67-68	2	28
β-strand	74-75	2	28
α-helix	81-112	32
α-helix	118-128	11
α-helix	136-150	15
α-helix	152-154	3
α-helix	159-166	8
α-helix	171-181	11
α-helix	187-194	8
α-helix	199-202	4
α-helix	203-207	5
α-helix	208-228	21
α-helix	231-236	6
α-helix	240-242	3
α-helix	245-248	4
α-helix	249-252	4
β-strand	253	1	29
β-strand	258	1	29
α-helix	260-281	22
α-helix	282-284	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ABC transporter related protein	A, B	protein	381	Escherichia coli	P68187 (AlphaFold model)
Maltose-binding periplasmic protein	E	protein	380	Escherichia coli	P0AEX9 (AlphaFold model)
Maltose transport system permease protein MalF	F	protein	514	Escherichia coli	P02916 (AlphaFold model)
Binding-protein-dependent transport systems inner membrane component	G	protein	296	Escherichia coli	P68183 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>4KI0_1 ABC transporter related protein (chains A, B)
MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL
FIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEV
LQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLH
KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMN
FLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVIL
EGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGT
ACRRLHKEPGVASASHHHHHH

Sequence of entity 2 (E), FASTA

>4KI0_2 Maltose-binding periplasmic protein (chains E)
KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDII
FWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD
LLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKD
VGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG
AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEA
LKDAQTRITKASASHHHHHH

Sequence of entity 3 (F), FASTA

>4KI0_3 Maltose transport system permease protein MalF (chains F)
MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANR
KAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTY
NFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNR
QALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSI
TADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGM
VLACLVQWEALRGKAVYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGVKPA
WFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFFKITLP
LLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVNYTYRIAFEGGG
GQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD

Sequence of entity 4 (G), FASTA

>4KI0_4 Binding-protein-dependent transport systems inner membrane component (chains G)
MAMVQPKSQKARLFITHLLLLLFIAAIMFPLLMVVAISLRQGNFATGSLIPEQISWDHWK
LALGFSVEQADGRITPPPFPVLLWLWNSVKVAGISAIGIVALSTTCAYAFARMRFPGKAT
LLKGMLIFQMFPAVLSLVALYALFDRLGEYIPFIGLNTHGGVIFAYLGGIALHVWTIKGY
FETIDSSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDV
NSYTLAVGMQQYLNPQNYLWGDFAAAAVMSALPITIVFLLAQRWLVNGLTAGGVKG

Ligands and cofactors

ID	Name	Formula	Copies
UMQ	Undecyl-maltoside	C23 H44 O11	11
PGV	(1R)-2-{[{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(palmitoylo…	C40 H77 O10 P	2
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	2
MG	Magnesium ion	Mg	2

Primary citation

Structural basis for substrate specificity in the Escherichia coli maltose transport system. Oldham, M.L., Chen, S., Chen, J. Proc Natl Acad Sci U S A (2013) 110:18132-18137. DOI 10.1073/pnas.1311407110 · PubMed

Other PDB entries of the same protein (UniProt P68187 (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…
2AWN 2.3 Å, Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ATP-Mg)
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
3PUV 2.4 Å, Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-VO4
1Q12 2.6 Å, Crystal Structure of the ATP-bound E. coli MalK
3GD7 2.7 Å, Crystal structure of human NBD2 complexed with N6-Phenylethyl-ATP (P-ATP)
1Q1B 2.8 Å, Crystal structure of E. coli MalK in the nucleotide-free form
2AWO 2.8 Å, Crystal structure of the ADP-Mg-bound E. Coli MALK (Crystallized with ADP-Mg)
1Q1E 2.9 Å, The ATPase component of E. coli maltose transporter (MalK) in the nucleotide-free form
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…

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