7KRU: PDB entry 7KRU

Name: PDB 7KRU: Stimulating state of a truncated Hsp70 DnaK fused with a substrate peptide
Published: 2021-09-15
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Stimulating state of a truncated Hsp70 DnaK fused with a substrate peptide. Determined by X-ray diffraction at 1.82 Å resolution. Released 15 Sept 2021.

Method: X-ray diffraction
Resolution: 1.82 Å
Organisms: Escherichia coli (strain K12), Escherichia coli K-12
Chains: 2
Atoms: 9,130
Mol. weight: 121.6 kDa
Ligands: ATP, MG, PDO
Released: 15 Sept 2021

Explore 7KRU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7KRU contains 49 α-helices and 71 β-strands across 2 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: 24 helices, 35 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	12
β-strand	13-20	8	12
β-strand	23-26	4	12
α-helix	27-28	2
β-strand	36-37	2	12
β-strand	39-42	4	13
β-strand	48-50	3	13
α-helix	52-57	6
α-helix	58-60	3
α-helix	62-64	3
β-strand	65-67	3	13
α-helix	69-71	3
β-strand	76	1	14
α-helix	80-88	9
β-strand	92-95	4	15
β-strand	100	1	14
β-strand	101-105	5	15
β-strand	108-110	3	15
α-helix	112-131	20
β-strand	137-142	6	12
α-helix	148-160	13
β-strand	164-170	7	12
α-helix	171-179	9
β-strand	188-195	8	16
β-strand	200-210	11	16
β-strand	213-224	12	16
α-helix	229-248	20
α-helix	252-254	3
α-helix	256-272	17
β-strand	278-289	12	17
β-strand	292-301	10	17
α-helix	302-314	13
α-helix	317-327	11
α-helix	331-333	3
β-strand	336-340	5	16
α-helix	342-345	4
α-helix	347-357	11
α-helix	360-362	3
α-helix	370-383	14
β-strand	389-391	3	16
β-strand	394	1	18
β-strand	399-403	5	19
β-strand	407-412	6	19
β-strand	417	1	18
β-strand	420-426	7	20
β-strand	427-428	2	21
β-strand	435-442	8	19
β-strand	447	1	19
α-helix	448-450	3
β-strand	452-460	9	19
α-helix	462-463	2
β-strand	472-478	7	20
β-strand	484-490	7	20
β-strand	496-501	6	20
α-helix	502-504	3
β-strand	506	1	16
α-helix	509-521	13
α-helix	523-532	10
β-strand	549-550	2	21

Chain B: 25 helices, 36 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	1
β-strand	13-14	2	2
β-strand	15-20	6	1
β-strand	23-26	4	1
α-helix	27-28	2
β-strand	36-37	2	2
β-strand	39-42	4	3
β-strand	48-50	3	3
α-helix	52-56	5
α-helix	58-60	3
α-helix	62-64	3
β-strand	65-67	3	3
α-helix	69-71	3
β-strand	76	1	4
α-helix	80-88	9
β-strand	92-95	4	5
β-strand	100	1	4
β-strand	101-105	5	5
β-strand	108-110	3	5
α-helix	112-131	20
β-strand	137-142	6	1
α-helix	148-160	13
β-strand	164-170	7	1
α-helix	171-179	9
β-strand	188-195	8	6
β-strand	200-210	11	6
β-strand	213-224	12	6
α-helix	229-248	20
α-helix	252-254	3
α-helix	256-272	17
β-strand	278-289	12	7
β-strand	292-301	10	7
α-helix	302-315	14
α-helix	317-327	11
α-helix	331-333	3
β-strand	336-340	5	6
α-helix	342-345	4
α-helix	347-357	11
α-helix	360-362	3
α-helix	370-383	14
β-strand	389-391	3	6
β-strand	394	1	8
β-strand	399-403	5	9
β-strand	407-412	6	9
α-helix	416	1
β-strand	417	1	8
β-strand	420-426	7	10
β-strand	427-428	2	11
β-strand	436-442	7	9
β-strand	447	1	9
α-helix	448-450	3
β-strand	452-459	8	9
α-helix	462-463	2
β-strand	472-478	7	10
β-strand	484-490	7	10
β-strand	496-501	6	10
α-helix	502-504	3
β-strand	506	1	6
α-helix	509-521	13
α-helix	523-534	12
β-strand	549-550	2	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chaperone protein DnaK fused with substrate peptide	A, B	protein	552	Escherichia coli (strain K12), Escherichia coli K-12	P0A6Y8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7KRU_1 Chaperone protein DnaK fused with substrate peptide (chains A, B)
MGKIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVT
NPQNTLFAIKRLIGRRFQDEEVQRDVSIMPFKIIAADNGDAWVEVKGQKMAPPQISAEVL
KKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYG
LDKGTGNRTIAVYDLGGGAFDISIIEIDEVDGEKTFEVLATNGDTHLGGEDFDSRLINYL
VEEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKV
TRAKLESLVEDLVNRSIEPLKVALQDAGLSVSDIDDVILVGGQTRMPMVQKKVAEFFGKE
PRKDVNPDEAVAIGAAVQGGVLTGDVKDVLLLDVTPLSLGIETMGGVMTTLIAKNTTIPT
KHSQVFSTAEDNQSAVTIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDA
DGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGD
TTGSGNRLLLTG

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
MG	Magnesium ion	Mg	2
PDO	1,3-propandiol	C3 H8 O2	2

Water and common crystallization additives (GOL, SO4) are not listed.

Primary citation

Conformational equilibria in allosteric control of Hsp70 chaperones. Wang, W., Liu, Q., Liu, Q. et al. Mol Cell (2021) 81:3919. DOI 10.1016/j.molcel.2021.07.039 · PubMed

Other PDB entries of the same protein (UniProt P0A6Y8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4F01 1.4 Å, Crystal structure of an artificial dimeric DnaK complex
7RAX 1.41 Å, ATP-binding state of the nucleotide-binding domain of Hsp70 DnaK mutant T199A
13JG 1.52 Å, E. coli DnaK bound to peptide PA1, structure B
4HY9 1.55 Å, Crystal structure of the substrate binding domain of E.coli DnaK in complex with…
4JNF 1.62 Å, Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP
4EZP 1.65 Å, Crystal structure of the substrate binding domain of E.coli DnaK in complex with…
4EZX 1.7 Å, Crystal structure of the substrate binding domain of E.coli DnaK in complex with the…
4HYB 1.7 Å, Crystal structure of the substrate binding domain of E.coli DnaK in complex with…
4R5K 1.75 Å, Crystal structure of the DnaK C-terminus (Dnak-SBD-B)
4EZN 1.8 Å, Crystal structure of the substrate binding domain of E.coli DnaK in complex with…
4EZW 1.8 Å, Crystal structure of the substrate binding domain of E.coli DnaK in complex with the…
4JWC 1.8 Å, Crystal structure of the substrate binding domain of E.coli DnaK in complex with bovine…

Browse structure collections

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