3PUZ: PDB entry 3PUZ

Crystal Structure of a pre-translocation state MBP-Maltose transporter complex bound to AMP-PNP. Determined by X-ray diffraction at 2.9 Å resolution. Released 18 May 2011.

Method: X-ray diffraction
Resolution: 2.9 Å
Organism: Escherichia coli
Chains: 5
Atoms: 14,697
Mol. weight: 216.98 kDa
Ligands: ANP, MG, PGV
Released: 18 May 2011

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

Secondary structure: helices and β-sheets

3PUZ contains 99 α-helices and 102 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: 14 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	19
β-strand	16-25	10	19
β-strand	31-35	5	20
α-helix	42-50	9
β-strand	57-62	6	19
β-strand	66	1	19
α-helix	72-74	3
β-strand	77-80	4	20
α-helix	92-101	10
α-helix	107-119	13
α-helix	124-126	3
α-helix	136-150	15
β-strand	154-158	5	20
α-helix	166-183	18
β-strand	186-191	6	20
α-helix	194-200	7
β-strand	203-208	6	20
β-strand	211-216	6	20
α-helix	218-223	6
β-strand	227	1	21
α-helix	228-233	6
α-helix	238-239	2
β-strand	240-250	11	22
β-strand	253-257	5	22
β-strand	265-268	4	22
β-strand	270	1	23
β-strand	280-285	6	22
β-strand	291-292	2	24
β-strand	299-309	11	24
β-strand	313-319	7	24
α-helix	326	1
β-strand	327-332	6	24
β-strand	342-346	5	24
α-helix	349-351	3
β-strand	353-355	3	22
β-strand	360	1	21
β-strand	361-362	2	22
α-helix	363	1
β-strand	364	1	23

Chain B: 12 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	25
β-strand	16-26	11	25
β-strand	31-35	5	26
α-helix	42-50	9
β-strand	57-62	6	25
β-strand	65-66	2	25
α-helix	72-75	4
β-strand	77-80	4	26
α-helix	92-101	10
α-helix	107-120	14
α-helix	136-150	15
β-strand	154-158	5	26
α-helix	166-183	18
β-strand	186-191	6	26
α-helix	194-200	7
β-strand	203-208	6	26
β-strand	211-216	6	26
α-helix	218-223	6
β-strand	227	1	27
α-helix	228-233	6
α-helix	238-239	2
β-strand	240-249	10	28
β-strand	254-257	4	28
β-strand	265-268	4	28
β-strand	270	1	29
β-strand	280-285	6	28
β-strand	291-292	2	30
β-strand	299-309	11	30
β-strand	313-319	7	30
β-strand	327-332	6	30
β-strand	342-346	5	30
α-helix	349-351	3
β-strand	352-355	4	28
β-strand	360	1	27
β-strand	361	1	28
α-helix	362-363	2
β-strand	364	1	29

Chain E: 24 helices, 25 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	7-10	4	1
α-helix	17-31	15
β-strand	35-38	4	1
α-helix	43-51	9
β-strand	59-63	5	1
α-helix	64-72	9
β-strand	76-77	2	1
α-helix	78-79	2
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	105-111	7	1
β-strand	114-118	5	4
β-strand	128	1	5
α-helix	132-140	9
β-strand	145-147	3	4
α-helix	154-161	8
β-strand	167	1	6
β-strand	170-171	2	7
β-strand	176-177	2	7
β-strand	182	1	6
α-helix	186-200	15
α-helix	210-218	9
β-strand	222-227	6	4
α-helix	229-231	3
α-helix	232-237	6
β-strand	242-245	4	4
α-helix	246-248	3
β-strand	249	1	5
β-strand	250	1	8
β-strand	253	1	8
α-helix	254-255	2
α-helix	257-258	2
β-strand	259	1	9
β-strand	260-267	8	1
α-helix	273-279	7
α-helix	280-284	5
α-helix	287-296	10
β-strand	301-302	2	1
β-strand	304	1	2
α-helix	305-311	7
α-helix	315-326	12
β-strand	329	1	9
α-helix	330-331	2
α-helix	337-352	16
α-helix	357-369	13

Chain F: 29 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	20-26	7
α-helix	31-35	5
α-helix	40-57	18
α-helix	64-66	3
α-helix	69-75	7
α-helix	76-80	5
α-helix	81-90	10
β-strand	92	1	10
β-strand	95	1	11
β-strand	100	1	12
α-helix	102-111	10
β-strand	113-121	9	13
β-strand	123-127	5	14
β-strand	130-136	7	14
β-strand	143-145	3	14
α-helix	146-148	3
β-strand	149	1	14
β-strand	155-158	4	13
β-strand	160-162	3	14
α-helix	165-166	2
α-helix	169-172	4
α-helix	173-178	6
α-helix	180-184	5
β-strand	186-189	4	13
β-strand	195-198	4	13
β-strand	203-209	7	13
β-strand	211-213	3	15
β-strand	219-221	3	15
β-strand	227-231	5	15
β-strand	236-239	4	15
β-strand	250-251	2	15
β-strand	255	1	12
β-strand	258	1	10
α-helix	262-269	8
α-helix	274-306	33
α-helix	314-322	9
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	398-406	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	16
α-helix	454	1
β-strand	462	1	16
α-helix	467-476	10
β-strand	483	1	11
α-helix	484-498	15

Chain G: 20 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	10-37	28
β-strand	40	1	17
β-strand	54	1	17
α-helix	57-62	6
β-strand	67-68	2	18
β-strand	74-75	2	18
α-helix	76-77	2
α-helix	81-111	31
α-helix	118-130	13
α-helix	133-136	4
α-helix	137-148	12
α-helix	152-154	3
α-helix	159-166	8
α-helix	171-181	11
α-helix	186-195	10
α-helix	199-202	4
α-helix	203-207	5
α-helix	212-227	16
α-helix	231-236	6
α-helix	240-242	3
α-helix	245-248	4
α-helix	249-251	3
α-helix	260-269	10
α-helix	272-280	9

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

>3PUZ_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

>3PUZ_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

>3PUZ_3 Maltose transporter subunit; membrane component of ABC superfamily (chains G)
MAMVQPKSQKARLFITHLLLLLFIAAIMFPLLMVVAISLRQGNFATGSLIPEQISWDHWK
LALGFSVEQADGRITPPPFPVLLWLWNSVKVAGISAIGIVALSTTCAYAFARMRFPGKAT
LLKGMLIFQMFPAVLSLVALYALFDRLGEYIPFIGLNTHGGVIFAYLGGIALHVWTIKGY
FETIDSSLEEAAALDGATPWQAFRLVLLPLSVPILAVVFILSFIAAITEVPVASLLLRDV
NSYTLAVGMQQYLNPQNYLWGDFAAAAVMSALPITIVFLLAQRWLVNGLTAGGVKG

Sequence of entity 4 (A, B), FASTA

>3PUZ_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
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	2
MG	Magnesium ion	Mg	2
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

Browse structure collections

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