4RZS: Lac repressor

Name: PDB 4RZS: Lac repressor engineered to bind sucralose, unliganded tetramer
Published: 2015-12-23
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transcription

Lac repressor engineered to bind sucralose, unliganded tetramer. Determined by X-ray diffraction at 2.71 Å resolution. Released 23 Dec 2015.

Method: X-ray diffraction
Resolution: 2.71 Å
Organism: Escherichia coli
Chains: 4
Atoms: 9,530
Mol. weight: 163.9 kDa
Released: 23 Dec 2015

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

Secondary structure: helices and β-sheets

4RZS contains 48 α-helices and 62 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: 14 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	6-13	8
α-helix	17-25	9
α-helix	35-43	9
β-strand	63-69	7	1
α-helix	74-89	16
β-strand	93-99	7	1
α-helix	104-116	13
β-strand	121-125	5	1
α-helix	130-140	11
β-strand	145-147	3	1
β-strand	158-161	4	1
α-helix	163-176	14
β-strand	182-186	5	2
α-helix	192-207	16
β-strand	214-217	4	2
α-helix	222-234	13
β-strand	241-244	4	2
α-helix	247-259	13
β-strand	264	1	3
β-strand	268	1	3
β-strand	269-271	3	2
β-strand	274	1	4
α-helix	277-281	5
β-strand	288-290	3	4
α-helix	293-307	15
β-strand	316-319	4	1
β-strand	322-324	3	4
α-helix	336-338	3
α-helix	339-354	16

Chain B: 14 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	6-13	8
α-helix	17-23	7
α-helix	35-43	9
α-helix	49	1
β-strand	63-69	7	5
α-helix	74-89	16
β-strand	93-99	7	5
α-helix	104-116	13
β-strand	121-125	5	5
β-strand	128	1	6
α-helix	130-139	10
β-strand	145-147	3	5
β-strand	150	1	6
β-strand	158-161	4	5
α-helix	163-176	14
β-strand	182-186	5	7
α-helix	192-206	15
β-strand	214-217	4	7
α-helix	222-234	13
β-strand	241-244	4	7
α-helix	247-259	13
β-strand	264	1	8
β-strand	268	1	8
β-strand	269-271	3	7
β-strand	274	1	9
α-helix	277-281	5
β-strand	288-290	3	9
α-helix	293-307	15
β-strand	316-319	4	5
β-strand	322-324	3	9
α-helix	339-354	16

Chain C: 10 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	63-69	7	10
α-helix	74-89	16
β-strand	93-99	7	10
α-helix	104-116	13
β-strand	121-125	5	10
α-helix	130-139	10
β-strand	145-147	3	10
β-strand	158-161	4	10
α-helix	163-176	14
β-strand	182-186	5	11
α-helix	192-207	16
β-strand	214-217	4	11
α-helix	222-234	13
β-strand	241-244	4	11
α-helix	247-259	13
β-strand	264	1	12
β-strand	268	1	12
β-strand	269-271	3	11
β-strand	274	1	13
α-helix	277-281	5
β-strand	288-290	3	13
α-helix	293-307	15
β-strand	316-319	4	10
β-strand	322-324	3	13
α-helix	339-354	16

Chain D: 10 helices, 15 β-strands

Element	Residues	Length	Sheet
β-strand	63-68	6	14
α-helix	74-89	16
β-strand	93-98	6	14
α-helix	104-116	13
β-strand	121-125	5	14
α-helix	130-140	11
β-strand	145-147	3	14
β-strand	158-161	4	14
α-helix	163-176	14
β-strand	182-186	5	15
α-helix	192-207	16
β-strand	214-217	4	15
α-helix	222-234	13
β-strand	241-244	4	15
α-helix	247-259	13
β-strand	264	1	16
β-strand	268	1	16
β-strand	269-271	3	15
β-strand	274	1	17
α-helix	277-281	5
β-strand	288-290	3	17
α-helix	293-307	15
β-strand	316-319	4	14
β-strand	322-324	3	17
α-helix	339-355	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Lac repressor	A, B, C, D	protein	381	Escherichia coli	P03023 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4RZS_1 Lac repressor (chains A, B, C, D)
MGSSHHHHHHSSGLVPRGSHMVKPVTLYDVAEYAGVSYQTVSRVVNQASHVSAKTREKVE
AAMAELNYIPNRVAQQLAGKQSLLIGVATSSLALHAPSQIVAAIKSRADQLGASVVVSMV
ERSGVEACKAAVHNLLAQRVSGLIINYPLDDQDAIAVEAACTNVPALFLTASDQTPLNSI
IFSHEDGTRLGVEHLVALGHQQIALLAGPLSSVDARLRLAGWHKYLTRNQIQPIAEREGD
WSAMSGFQQTMQMLNEGIVPTAMLVANDQMALGAMRAITESGLRVGADISVVGYDDTEDS
SCYIPPLTTIKQDFRLLGQTSVDRLLQLSQGQAVKGNQLLPVSLVKRKTTLAPNTQTASP
RALADSLMQLARQVSRLESGQ

Primary citation

Engineering an allosteric transcription factor to respond to new ligands. Taylor, N.D., Garruss, A.S., Moretti, R. et al. Nat Methods (2016) 13:177-183. DOI 10.1038/nmeth.3696 · PubMed

Other PDB entries of the same protein (UniProt P03023 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8GOH 1.1 Å, Homotetramic Antiparallel Coiled-Coil of 23-residues LacI C-terminal tetramerization helix
1JYE 1.7 Å, Structure of a Dimeric Lac Repressor with C-terminal Deletion and K84L Substitution
2P9H 2.0 Å, High resolution structure of the Lactose Repressor bound to IPTG
3EDC 2.1 Å, Crystal Structure of a 1.6-hexanediol Bound Tetrameric Form of Escherichia coli…
1EFA 2.6 Å, Crystal structure of the lac repressor dimer bound to operator and the anti-inducer onpf
1TLF 2.6 Å, Unprecedented quaternary structure of E. Coli lac repressor core tetramer: implications…
1LBI 2.7 Å, Lac repressor
1JYF 3.0 Å, Structure of the Dimeric Lac Repressor with an 11-residue C-terminal Deletion.
4RZT 3.1 Å, Lac repressor engineered to bind sucralose, sucralose-bound tetramer
1LBH 3.2 Å, Intact lactose operon repressor with gratuitous inducer iptg
2PAF 3.5 Å, Crystal Structure of the Lactose Repressor bound to anti-inducer ONPF in induced state
2PE5 3.5 Å, Crystal Structure of the Lac Repressor bound to ONPG in repressed state

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