6SR6: RAC core with a pseudo substrate

Crystal structure of the RAC core with a pseudo substrate bound to Ssz1 SBD. Determined by X-ray diffraction at 2.5 Å resolution. Released 25 Mar 2020.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Chains: 4
Atoms: 8,887
Mol. weight: 142.29 kDa
Ligands: ATP, MG
Released: 25 Mar 2020

Explore 6SR6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6SR6 contains 60 α-helices and 69 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: 25 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	10-12	3
β-strand	15-20	6	1
β-strand	24-31	8	1
β-strand	34-38	5	1
α-helix	39	1
β-strand	47-48	2	1
β-strand	50-54	5	2
β-strand	57-60	4	2
α-helix	61-66	6
α-helix	72-74	3
β-strand	75-77	3	2
α-helix	87-89	3
α-helix	93-95	3
α-helix	99-101	3
β-strand	102-104	3	3
β-strand	107-112	6	3
α-helix	120-122	3
β-strand	123-126	4	3
α-helix	127-146	20
β-strand	152-157	6	1
α-helix	163-175	13
β-strand	179-185	7	1
α-helix	186-195	10
β-strand	205-212	8	4
β-strand	217-225	9	4
β-strand	228-237	10	4
α-helix	242-260	19
α-helix	264-266	3
α-helix	267-269	3
α-helix	271-290	20
β-strand	293-302	10	5
β-strand	305-312	8	5
α-helix	313-319	7
α-helix	321-337	17
α-helix	342-344	3
β-strand	347-351	5	4
α-helix	353-356	4
α-helix	358-367	10
β-strand	373-375	3	4
α-helix	389-401	13
α-helix	406-412	7
α-helix	415-418	4
β-strand	419-423	5	6
β-strand	426-430	5	7
β-strand	440-444	5	7
α-helix	445	1
β-strand	448-449	2	6
β-strand	452-459	8	8
β-strand	465-479	15	7
β-strand	524-541	18	7
α-helix	542	1
β-strand	546-553	8	8
β-strand	559-562	4	8
β-strand	565	1	8
β-strand	573-576	4	8

Chain B: 4 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	8
α-helix	10-11	2
β-strand	12	1	7
α-helix	13-14	2
α-helix	20-22	3
β-strand	23-25	3	7
β-strand	34-38	5	6
β-strand	39	1	4
α-helix	44-53	10

Chain C: 25 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	15-20	6	9
β-strand	24-31	8	9
β-strand	34-38	5	9
α-helix	39	1
β-strand	47-48	2	9
β-strand	50-54	5	10
β-strand	57-60	4	10
α-helix	61-66	6
α-helix	72-74	3
β-strand	75-77	3	10
α-helix	87-89	3
α-helix	93-95	3
α-helix	99-101	3
β-strand	102-104	3	11
β-strand	107-112	6	11
α-helix	120-122	3
β-strand	123-126	4	11
α-helix	127-146	20
β-strand	152-157	6	9
α-helix	163-175	13
β-strand	179-185	7	9
α-helix	186-195	10
β-strand	205-212	8	12
β-strand	217-225	9	12
β-strand	228-237	10	12
α-helix	242-260	19
α-helix	264-266	3
α-helix	267-269	3
α-helix	271-290	20
β-strand	293-302	10	13
β-strand	305-312	8	13
α-helix	313-319	7
α-helix	321-337	17
α-helix	342-344	3
β-strand	347-351	5	12
α-helix	353-356	4
α-helix	358-367	10
β-strand	373-375	3	12
α-helix	383-385	3
α-helix	389-401	13
α-helix	406-412	7
α-helix	415-418	4
β-strand	419-423	5	14
β-strand	426-430	5	15
β-strand	440-444	5	15
β-strand	448-449	2	14
β-strand	452-459	8	16
α-helix	460-461	2
β-strand	465-479	15	15
β-strand	524-541	18	15
α-helix	542	1
β-strand	546-553	8	16
β-strand	559-565	7	16
β-strand	571-576	6	16

Chain D: 6 helices, 5 β-strands

Element	Residues	Length	Sheet
β-strand	4-9	6	16
α-helix	10-11	2
β-strand	12	1	15
α-helix	13-14	2
α-helix	20-22	3
β-strand	23-25	3	15
α-helix	31-33	3
β-strand	34-38	5	14
β-strand	39	1	12
α-helix	40	1
α-helix	44-53	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Putative heat shock protein	A, C	protein	589	Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)	G0RZX9 (AlphaFold model)
Putative ribosome associated protein	B, D	protein	63	Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)	G0RYD6 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6SR6_1 Putative heat shock protein (chains A, C)
SAMGWSHPQFEKAESASKAAPGERVVIGITFGNSNSSIAHTVDDKAEVIANEDGDRQIPT
ILSYVDGDEYYGQQAKNFLVRNPKNTVAYFRDILGQDFKSVDPTHNHASAHPQEAGDNVV
FTIKDKAEEDAEPSTLTVSEIATRYLRRLVGAASEYLGKKVTSAVITIPTNFTEKQKAAL
IAAAAAADLEVLQLISEPAAAVLAYDARPEATISDKIIVVADLGGSRSDVTVLASRSGMY
TILATVHDYEYHGIALDKVLIDHFSKEFLKKNPGAKDPRENPRSLAKLRLEAESTKRALS
RSTNASFSVESLIDGLDFASTINRLRYETIARTVFEGFNRLVESAVKKAGLDPLDVDEVI
MSGGTSNTPRIAANFRYIFPESTRILAPSTDPSALNPSELQARGAALQASLIQEFETEDI
EQSTHAAVTTMPHVTNAIGVVSVSESGEEKFVPIIAPETAVPARRTVHLDAPKEGGDVLV
KVVEGSTHINVIKPEPKAKEDGETKEKTEDADDDGDFDDDDEEEEEEEEEEEKREKVWKI
GSTLAEAAVRGVKKGAKVEVTINVNTDLTVIVTAREVGGKGGVRGTLSA

Sequence of entity 2 (B, D), FASTA

>6SR6_2 Putative ribosome associated protein (chains B, D)
GPAMNATVVSLPLPTLPEGWAAEKDFKAIGKLTQEGSSMRTLEPVGPHFLAHARRVRHKR
TFS

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
MG	Magnesium ion	Mg	2

Primary citation

The ribosome-associated complex RAC serves in a relay that directs nascent chains to Ssb. Zhang, Y., Valentin Gese, G., Conz, C. et al. Nat Commun (2020) 11:1504-1504. DOI 10.1038/s41467-020-15313-w · PubMed

Other PDB entries of the same protein (UniProt G0RZX9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4GNI 1.8 Å, Structure of the Ssz1 ATPase bound to ATP and Magnesium
5MB9 3.2 Å, Crystal structure of the eukaryotic ribosome associated complex (RAC), a unique…
7Z3N 3.2 Å, Cryo-EM structure of the ribosome-associated RAC complex on the 80S ribosome - RAC-1…
7Z3O 3.3 Å, Cryo-EM structure of the ribosome-associated RAC complex on the 80S ribosome - RAC-2…

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