3BP8: Mlc/EIIB complex

Crystal structure of Mlc/EIIB complex. Determined by X-ray diffraction at 2.85 Å resolution. Released 27 May 2008.

Method: X-ray diffraction
Resolution: 2.85 Å
Organism: Escherichia coli
Chains: 4
Atoms: 6,943
Mol. weight: 104.51 kDa
Ligands: ZN
Released: 27 May 2008

Explore 3BP8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BP8 contains 41 α-helices and 47 β-strands across 4 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: 16 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	14-27	14
β-strand	31	1	1
α-helix	33-39	7
α-helix	44-56	13
β-strand	60-62	3	1
β-strand	78-80	3	1
β-strand	85-92	8	2
β-strand	96-103	8	2
β-strand	108-115	8	2
α-helix	124-138	15
β-strand	145-153	9	2
β-strand	156-158	3	3
β-strand	163-166	4	3
β-strand	176	1	3
α-helix	181-184	4
β-strand	190-194	5	2
α-helix	195-205	11
β-strand	215-220	6	4
β-strand	224-230	7	4
β-strand	233-234	2	4
α-helix	245-247	3
β-strand	256	1	5
β-strand	262	1	5
α-helix	271-279	9
α-helix	297-306	10
α-helix	309-333	25
β-strand	337-341	5	4
α-helix	343-347	5
α-helix	348-362	15
α-helix	365-368	4
β-strand	373-375	3	4
α-helix	383-386	4
α-helix	387-395	9
α-helix	400-403	4

Chain B: 17 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	13-24	12
α-helix	33-39	7
α-helix	49-55	7
β-strand	60-62	3	6
β-strand	78-80	3	6
β-strand	86-92	7	7
β-strand	96	1	8
β-strand	97-102	6	7
β-strand	108-111	4	7
β-strand	115	1	8
α-helix	125-138	14
β-strand	146-152	7	7
β-strand	157	1	9
β-strand	164	1	9
β-strand	176	1	9
α-helix	178-184	7
β-strand	190-193	4	7
α-helix	195-205	11
β-strand	215-220	6	10
β-strand	224-230	7	10
β-strand	233-234	2	10
α-helix	235	1
α-helix	245-247	3
β-strand	249	1	11
β-strand	256	1	12
β-strand	262	1	12
β-strand	264	1	11
α-helix	265-268	4
α-helix	271-282	12
α-helix	297-304	8
α-helix	309-333	25
β-strand	337-341	5	10
α-helix	343-347	5
α-helix	352-361	10
α-helix	365-368	4
β-strand	373-375	3	10
α-helix	388-395	8
α-helix	398-404	7

Chain C: 4 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	14-20	7
β-strand	27-30	4	13
β-strand	37-41	5	13
α-helix	44-46	3
α-helix	49-55	7
β-strand	60-63	4	13
β-strand	66-69	4	13
α-helix	75-85	11

Chain D: 4 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	19-21	3
β-strand	27-29	3	14
β-strand	38-41	4	14
α-helix	44-46	3
α-helix	49-53	5
β-strand	60-63	4	14
β-strand	66-69	4	14
α-helix	74-84	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Putative NAGC-like transcriptional regulator	A, B	protein	406	Escherichia coli	P50456 (AlphaFold model)
PTS system glucose-specific EIICB component	C, D	protein	75	Escherichia coli	P69786 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3BP8_1 Putative NAGC-like transcriptional regulator (chains A, B)
MVAENQPGHIDQIKQTNAGAVYRLIDQLGPVSRIDLSRLAQLAPASITKIVREMLEAHLV
QELEIKEAGNRGRPAVGLVVETEAWHYLSLRISRGEIFLALRDLSSKLVVEESQELALKD
DSPLLDRIISHIDQFFIRHQKKLERLTSIAITLPGIIDTENGIVHRMPFYEDVKEMPLGE
ALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSS
SLVEIGHTQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLNQSMSSMLHGQPLTVDSL
CQAALRGDLLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIR
QQALPAYSQHISVESTQFSNQGTMAGAALVKDAMYNGSLLIRLLQG

Sequence of entity 2 (C, D), FASTA

>3BP8_2 PTS system glucose-specific EIICB component (chains C, D)
MAPALVAAFGGKENITNLDACITRLRVSVADVSKVDQAGLKKLGAAGVVVAGSGVQAIFG
TKSDNLKTEMDEYIR

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	2

Water and common crystallization additives (ACT) are not listed.

Primary citation

Analyses of Mlc-IIBGlc interaction and a plausible molecular mechanism of Mlc inactivation by membrane sequestration. Nam, T.W., Jung, H.I., An, Y.J. et al. Proc Natl Acad Sci U S A (2008) 105:3751-3756. DOI 10.1073/pnas.0709295105 · PubMed

Other PDB entries of the same protein (UniProt P50456 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9SRW 2.3 Å, Cryo-EM structure of the Mlc tetramer in complex with the anti-repressor MtfA
9SRU 2.47 Å, Cryo-EM structure of Mlc in complex with ptsG operator DNA
1Z6R 2.7 Å, Crystal structure of Mlc from Escherichia coli
9SRT 2.74 Å, Cryo-EM structure of the Mlc tetramer
9SRX 2.96 Å, Cryo-EM structure of the Mlc repressor in complex with the glucose-specific IICB…

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