5YA0: LsrK and HPr complex

Crystal structure of LsrK and HPr complex. Determined by X-ray diffraction at 3.0 Å resolution. Released 11 Jul 2018.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Escherichia coli K-12
Chains: 4
Atoms: 8,657
Mol. weight: 136.77 kDa
Ligands: PO4, HEZ
Released: 11 Jul 2018

Explore 5YA0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5YA0 contains 58 α-helices and 52 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: 26 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	13-19	7	1
β-strand	24-29	6	1
β-strand	35-41	7	1
α-helix	56-58	3
α-helix	60-77	18
α-helix	81-83	3
β-strand	84-91	8	1
β-strand	96-99	4	2
β-strand	105-109	5	2
α-helix	117-129	13
α-helix	131-139	9
α-helix	148-157	10
α-helix	159-162	4
β-strand	167-170	4	2
α-helix	171-180	10
β-strand	185	1	3
α-helix	187-190	4
α-helix	191-193	3
β-strand	196-197	2	4
β-strand	202-203	2	4
α-helix	205-211	7
α-helix	215-218	4
β-strand	221	1	3
β-strand	227-230	4	1
α-helix	233-239	7
α-helix	241-242	2
β-strand	246-252	7	1
α-helix	253-261	9
β-strand	269-273	5	5
β-strand	277-283	7	5
β-strand	295-298	4	5
β-strand	305-311	7	5
α-helix	315-324	10
α-helix	327-336	10
α-helix	340-345	6
α-helix	352	1
α-helix	355-357	3
β-strand	359-361	3	6
β-strand	377-379	3	6
α-helix	390-416	27
β-strand	423-426	4	5
α-helix	429-431	3
α-helix	433-443	11
β-strand	447-450	4	5
α-helix	456-468	13
α-helix	474-481	8
β-strand	484-488	5	5
α-helix	492-503	12

Chain B: 26 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	13-19	7	7
β-strand	24-29	6	7
β-strand	35-41	7	7
α-helix	56-58	3
α-helix	60-77	18
α-helix	81-83	3
β-strand	84-91	8	7
β-strand	96-99	4	8
β-strand	105-109	5	8
α-helix	117-129	13
α-helix	131-139	9
α-helix	148-157	10
α-helix	159-162	4
β-strand	167-170	4	8
α-helix	171-180	10
β-strand	185	1	9
α-helix	187-190	4
α-helix	191-193	3
β-strand	196-197	2	10
β-strand	202-203	2	10
α-helix	205-211	7
α-helix	215-218	4
β-strand	221	1	9
β-strand	227-230	4	7
α-helix	233-239	7
α-helix	241-242	2
β-strand	246-252	7	7
α-helix	253-261	9
β-strand	269-273	5	11
β-strand	277-283	7	11
β-strand	295-298	4	11
β-strand	305-311	7	11
α-helix	315-324	10
α-helix	329-336	8
α-helix	340-345	6
α-helix	352	1
α-helix	355-357	3
β-strand	359-361	3	12
β-strand	377-379	3	12
α-helix	390-416	27
β-strand	423-426	4	11
α-helix	429-431	3
α-helix	433-443	11
β-strand	447-450	4	11
α-helix	456-468	13
α-helix	474-481	8
β-strand	484-488	5	11
α-helix	492-501	10

Chains C and D: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	2-7	6	13
α-helix	16-26	11
β-strand	32-37	6	13
β-strand	40-43	4	13
α-helix	47-51	5
β-strand	60-66	7	13
α-helix	70-83	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Autoinducer-2 kinase	A, B	protein	540	Escherichia coli K-12	P77432 (AlphaFold model)
Phosphocarrier protein HPr	C, D	protein	85	Escherichia coli K-12	P0AA04 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5YA0_1 Autoinducer-2 kinase (chains A, B)
HHHHHHSEDPMARLFTLSESKYYLMALDAGTGSIRAVIFDLEGNQIAVGQAEWRHLAVPD
VPGSMEFDLNKNWQLACECMRQALHNAGIAPEYIAAVSACSMREGIVLYNNEGAPIWACA
NVDARAAREVSELKELHNNTFENEVYRATGQTLALSAIPRLLWLAHHRSDIYRQASTITM
ISDWLAYMLSGELAVDPSNAGTTGLLDLTTRDWKPALLDMAGLRADILSPVKETGTLLGV
VSSQAAELCGLKAGTPVVVGGGDVQLGCLGLGVVRPAQTAVLGGTFWQQVVNLAAPVTDP
EMNVRVNPHVIPGMVQAESISFFTGLTMRWFRDAFCAEEKLIAERLGIDTYTLLEEMASR
VPPGSWGVMPIFSDRMRFKTWYHAAPSFINLSIDPDKCNKATLFRALEENAAIVSACNLQ
QIADFSNIHPSSLVFAGGGSKGKLWSQILADVSGLPVNIPVVKEATALGCAIAAGVGAGI
FSSMAETGERLVRWERTHTPDPEKHELYQDSRDKWQAVYQDQLGLVDHGLTTSLWKAPGL

Sequence of entity 2 (C, D), FASTA

>5YA0_2 Phosphocarrier protein HPr (chains C, D)
MFQQEVTITAPNGLHTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTV
VTISAEGEDEQKAVEHLVKLMAELE

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	6
HEZ	Hexane-1,6-diol	C6 H14 O2	2

Primary citation

Evidence of link between quorum sensing and sugar metabolism inEscherichia colirevealed via cocrystal structures of LsrK and HPr. Ha, J.H., Hauk, P., Cho, K. et al. Sci Adv (2018) 4:eaar7063-eaar7063. DOI 10.1126/sciadv.aar7063 · PubMed

Other PDB entries of the same protein (UniProt P77432 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5YA1 2.7 Å, crystal structure of LsrK-HPr complex with ATP
5YA2 2.7 Å, Crystal structure of LsrK-HPr complex with ADP

Browse structure collections

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