3PV0: PDB entry 3PV0

Crystal Structure of a pre-translocation state MBP-Maltose transporter complex without nucleotide. Determined by X-ray diffraction at 3.1 Å resolution. Released 18 May 2011.

Method: X-ray diffraction
Resolution: 3.1 Å
Organism: Escherichia coli
Chains: 5
Atoms: 14,643
Mol. weight: 215.92 kDa
Ligands: PGV
Released: 18 May 2011

Explore 3PV0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3PV0 contains 98 α-helices and 107 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: 12 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	5-13	9	22
β-strand	16-25	10	22
β-strand	31-35	5	23
α-helix	42-50	9
β-strand	57-61	5	22
β-strand	66	1	22
α-helix	72-74	3
β-strand	77-80	4	23
α-helix	92-97	6
α-helix	107-121	15
α-helix	124-126	3
α-helix	138-150	13
β-strand	154-158	5	23
α-helix	166-183	18
β-strand	187-191	5	23
α-helix	194-200	7
β-strand	203-208	6	23
β-strand	211-216	6	23
α-helix	218-223	6
β-strand	227	1	24
α-helix	228-231	4
α-helix	238-239	2
β-strand	240-250	11	25
β-strand	253-257	5	25
β-strand	265-268	4	25
β-strand	270	1	26
β-strand	280-285	6	25
β-strand	291-292	2	27
β-strand	299-309	11	27
β-strand	313-319	7	27
β-strand	327-332	6	27
β-strand	342-346	5	27
α-helix	349-351	3
β-strand	353-355	3	25
β-strand	360	1	24
β-strand	361	1	25
β-strand	364	1	26

Chain B: 14 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	28
β-strand	16-25	10	28
β-strand	31-35	5	29
α-helix	42-50	9
β-strand	57-62	6	28
β-strand	66	1	28
α-helix	72-74	3
β-strand	77-80	4	29
α-helix	92-101	10
α-helix	107-120	14
α-helix	124-126	3
α-helix	136-150	15
β-strand	154-158	5	29
α-helix	166-183	18
β-strand	186-190	5	29
α-helix	194-200	7
β-strand	203-207	5	29
β-strand	212-216	5	29
α-helix	218-223	6
β-strand	227	1	30
α-helix	228-231	4
α-helix	238-239	2
β-strand	240-249	10	31
β-strand	254-257	4	31
β-strand	265-268	4	31
β-strand	270	1	32
β-strand	280-285	6	31
α-helix	287-289	3
β-strand	291-292	2	33
β-strand	299-309	11	33
β-strand	313-319	7	33
β-strand	327-332	6	33
β-strand	342-346	5	33
α-helix	349-351	3
β-strand	353-355	3	31
β-strand	360	1	30
β-strand	361	1	31
α-helix	362-363	2
β-strand	364	1	32

Chain E: 24 helices, 22 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	7-11	5	1
α-helix	17-31	15
α-helix	33-34	2
β-strand	35-38	4	1
α-helix	43-52	10
β-strand	59-63	5	1
α-helix	64-72	9
β-strand	76-77	2	1
α-helix	83-86	4
β-strand	89	1	2
α-helix	91-96	6
β-strand	98-99	2	3
β-strand	102-103	2	3
β-strand	106-111	6	1
β-strand	114-118	5	4
β-strand	128	1	5
α-helix	131-140	10
β-strand	145-147	3	4
α-helix	154-163	10
β-strand	167-172	6	6
β-strand	175-182	8	6
α-helix	186-200	15
α-helix	210-217	8
β-strand	222-227	6	4
α-helix	229-231	3
α-helix	232-238	7
β-strand	242-245	4	4
α-helix	246-248	3
β-strand	249-250	2	5
β-strand	253-254	2	5
α-helix	255	1
α-helix	257	1
β-strand	258-259	2	7
β-strand	260-267	8	1
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-294	8
β-strand	301-302	2	1
β-strand	304	1	2
α-helix	305-311	7
α-helix	315-326	12
β-strand	328-329	2	7
α-helix	330-331	2
α-helix	336-352	17
α-helix	357-369	13

Chain F: 29 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	20-23	4
α-helix	26-29	4
α-helix	32-35	4
α-helix	44-58	15
α-helix	69-75	7
α-helix	76-80	5
α-helix	81-88	8
β-strand	92	1	8
β-strand	95	1	9
β-strand	100	1	10
α-helix	102-111	10
β-strand	113-121	9	11
β-strand	123-124	2	12
β-strand	127	1	13
β-strand	130	1	13
β-strand	131	1	14
β-strand	133-136	4	12
β-strand	143-145	3	12
β-strand	149	1	14
β-strand	155	1	15
β-strand	158	1	16
β-strand	160-162	3	12
α-helix	165-166	2
α-helix	169-172	4
α-helix	173-178	6
α-helix	180-185	6
β-strand	186	1	15
β-strand	189	1	16
β-strand	195	1	16
β-strand	197-198	2	11
β-strand	203-209	7	11
β-strand	211-213	3	17
β-strand	219-221	3	17
β-strand	227-231	5	17
β-strand	236-239	4	17
β-strand	250-251	2	17
β-strand	255	1	10
β-strand	258	1	8
α-helix	262-269	8
α-helix	271-307	37
α-helix	314-320	7
α-helix	323-326	4
α-helix	329-339	11
α-helix	346-351	6
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	419-421	3
α-helix	423-438	16
α-helix	441-447	7
β-strand	453	1	18
α-helix	454	1
β-strand	462	1	18
α-helix	467-476	10
β-strand	483	1	9
α-helix	484-501	18

Chain G: 19 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	10-37	28
β-strand	40	1	19
β-strand	54	1	19
α-helix	57-63	7
β-strand	67-69	3	20
β-strand	73-75	3	20
α-helix	81-112	32
α-helix	118-128	11
α-helix	133-135	3
α-helix	137-150	14
α-helix	152-154	3
α-helix	159-166	8
α-helix	171-181	11
α-helix	186-194	9
α-helix	199-202	4
α-helix	203-207	5
α-helix	209-211	3
α-helix	212-228	17
α-helix	233-236	4
α-helix	240-242	3
α-helix	245-248	4
β-strand	253-254	2	21
β-strand	257-258	2	21
α-helix	260-270	11
α-helix	273-280	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Maltose transporter subunit; periplasmic-binding component of ABC superfamily	E	protein	370	Escherichia coli	P0AEX9 (AlphaFold model)
Maltose transporter subunit; membrane component of ABC superfamily	F	protein	514	Escherichia coli	P02916 (AlphaFold model)
Maltose transporter subunit; membrane component of ABC superfamily	G	protein	296	Escherichia coli	P68183 (AlphaFold model)
Fused maltose transport subunit, ATP-binding component of ABC superfamily; regulatory protein	A, B	protein	381	Escherichia coli	P68187 (AlphaFold model)

Sequence of entity 1 (E), FASTA

>3PV0_1 Maltose transporter subunit; periplasmic-binding component of ABC superfamily (chains E)
KIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDII
FWAHDRFGCYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKD
LLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKD
VGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKV
NYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLG
AVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMCAFWYAVRTAVINAASGRQTVDEA
LKDAQTRITK

Sequence of entity 2 (F), FASTA

>3PV0_2 Maltose transporter subunit; membrane component of ABC superfamily (chains F)
MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANR
KAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTY
NFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNR
QALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSI
TADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGM
VLACLVQWEALRGKAVYRVLLILPYAVPSFISILIFKGLFNQSFGEINMMLSALFGVKPA
WFSDPTTARTMLIIVNTWLGYPYMMILCMGLLKAIPDDLYEASAMDGAGPFQNFFKITLP
LLIKPLTPLMIASFAFNFNNFVLIQLLTNGGPDRLGTTTPAGYTDLLVNYTYRIAFEGGG
GQDFGLAAAIATLIFLLVGALAIVNLKATRMKFD

Sequence of entity 3 (G), FASTA

>3PV0_3 Maltose transporter subunit; membrane component of ABC superfamily (chains G)
MAMVQPKSQKARLFITHLLLLLFIAAIMFPLLMVVAISLRQGNFATGSLIPEQISWDHWK
LALGFSVEQADGRITPPPFPVLLWLWNSVKVAGISAIGIVALSTTCAYAFARMRFPGKAT
LLKGMLIFQMFPAVLSLVALYALFDRLGEYIPFIGLNTHGGVIFAYLGGIALHVWTIKGY
FETIDSSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDV
NSYTLAVGMQQYLNPQNYLWGDFAAAAVMSALPITIVFLLAQRWLVNGLTAGGVKG

Sequence of entity 4 (A, B), FASTA

>3PV0_4 Fused maltose transport subunit, ATP-binding component of ABC superfamily; regulatory protein (chains A, B)
MASVQLQNVTKAWGEVVVSKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLETITSGDL
FIGEKRMNDTPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEVINQRVNQVAEV
LQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLH
KRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPADRFVAGFIGSPKMN
FLPVKVTATAIDQVQVELPMPNRQQVWLPVESRDVQVGANMSLGIRPEHLLPSDIADVIL
EGEVQVVEQLGNETQIHIQIPSIRQNLVYRQNDVVLVEEGATFAIGLPPERCHLFREDGT
ACRRLHKEPGVASASHHHHHH

Ligands and cofactors

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

Primary citation

Crystal structure of the maltose transporter in a pretranslocation intermediate state. Oldham, M.L., Chen, J. Science (2011) 332:1202-1205. DOI 10.1126/science.1200767 · PubMed

Other PDB entries of the same protein (UniProt P0AEX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8C8F 1.15 Å, Crystal structure of the E. coli maltodextrin-binding protein
4EXK 1.28 Å, A chimera protein containing MBP fused to the C-terminal domain of the uncharacterized…
3Q27 1.3 Å, Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)
7KD4 1.31 Å, Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329…
5M13 1.37 Å, Synthetic nanobody in complex with MBP
5HZ7 1.43 Å, High-resolution crystal structure of the minor DNA-binding pilin ComP from Neisseria…
5H7Q 1.45 Å, Crystal structure of human MNDA PYD domain with MBP tag
6XDS 1.47 Å, Crystal structure of MBP-TREM2 Ig domain fusion with fragment,…
4IRL 1.47 Å, X-ray structure of the CARD domain of zebrafish GBP-NLRP1 like protein
8SVY 1.47 Å, MBP-Mcl1 in complex with ligand 10
3MP6 1.48 Å, Complex Structure of Sgf29 and dimethylated H3K4
9CLC 1.48 Å, Crystal structure of maltose binding protein (Apo), mutant Trp10 to 4-Cyanotryptophan

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