7OS2: Brr2

Cryo-EM structure of Brr2 in complex with Jab1/MPN and C9ORF78. Determined by electron microscopy at 2.76 Å resolution. Released 23 Feb 2022.

Method: Electron microscopy
Resolution: 2.76 Å
Organism: Homo sapiens
Chains: 3
Atoms: 16,485
Mol. weight: 264.73 kDa
Released: 23 Feb 2022

Explore 7OS2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7OS2 contains 117 α-helices and 85 β-strands across 3 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 B: 98 helices, 68 β-strands

Element	Residues	Length	Sheet
α-helix	411-414	4
α-helix	419-421	3
β-strand	435-439	5	1
β-strand	442-446	5	1
α-helix	448-455	8
α-helix	461-462	2
β-strand	463	1	2
α-helix	464-466	3
α-helix	469-472	4
β-strand	480	1	2
α-helix	483-493	11
β-strand	499-502	4	3
α-helix	509-522	14
α-helix	533-535	3
β-strand	537-541	5	3
α-helix	545-558	14
α-helix	560-562	3
β-strand	566-568	3	3
α-helix	573-582	10
β-strand	585-588	4	3
α-helix	590-599	10
β-strand	609-614	6	3
α-helix	617-621	5
α-helix	625-642	18
β-strand	647-652	6	3
α-helix	658-664	7
β-strand	673-675	3	3
α-helix	678-680	3
β-strand	688-692	5	1
α-helix	697-714	18
β-strand	721-724	4	1
α-helix	728-744	17
α-helix	749-753	5
α-helix	761-766	6
α-helix	774-777	4
α-helix	778-780	3
β-strand	782-785	4	1
α-helix	791-802	12
β-strand	808-811	4	1
α-helix	814-818	5
β-strand	823	1	4
β-strand	825-828	4	1
β-strand	832-835	4	5
β-strand	840-843	4	5
α-helix	844-845	2
α-helix	846-853	8
β-strand	856	1	4
β-strand	867-872	6	1
α-helix	873-875	3
α-helix	876-883	8
α-helix	897-907	11
β-strand	912	1	6
α-helix	913-920	8
α-helix	924-931	8
α-helix	933-936	4
α-helix	940-945	6
α-helix	950-966	17
β-strand	970-972	3	7
β-strand	978	1	6
β-strand	979-981	3	7
α-helix	983-991	9
α-helix	995-1004	10
α-helix	1011-1019	9
α-helix	1022-1024	3
α-helix	1035-1043	9
α-helix	1055-1068	14
α-helix	1075-1102	28
β-strand	1104	1	8
α-helix	1105-1120	16
α-helix	1128-1131	4
α-helix	1137-1145	9
α-helix	1150-1154	5
α-helix	1158-1164	7
α-helix	1171-1180	10
β-strand	1184-1194	11	9
β-strand	1197-1206	10	9
α-helix	1212-1215	4
β-strand	1218-1226	9	10
β-strand	1232	1	8
β-strand	1233-1242	10	10
β-strand	1250-1257	8	9
β-strand	1265-1272	8	10
β-strand	1279-1285	7	10
α-helix	1291-1298	8
β-strand	1299	1	11
α-helix	1300	1
α-helix	1305-1306	2
β-strand	1307-1308	2	12
α-helix	1309-1311	3
α-helix	1315-1322	8
β-strand	1327-1328	2	12
α-helix	1330-1336	7
α-helix	1337-1341	5
β-strand	1346-1349	4	13
α-helix	1357-1370	14
β-strand	1376-1379	4	13
α-helix	1383-1393	11
α-helix	1394-1398	5
β-strand	1405-1407	3	13
α-helix	1412-1421	10
β-strand	1424-1427	4	13
α-helix	1429-1436	8
α-helix	1443-1446	4
β-strand	1450-1454	5	13
α-helix	1456-1460	5
α-helix	1464-1481	18
β-strand	1486-1491	6	13
β-strand	1494	1	14
α-helix	1497-1504	8
β-strand	1511-1513	3	13
β-strand	1514	1	11
α-helix	1516-1518	3
β-strand	1523-1529	7	15
α-helix	1535-1541	7
α-helix	1543-1553	11
β-strand	1559-1563	5	15
α-helix	1566-1582	17
α-helix	1594-1601	8
α-helix	1607-1614	8
β-strand	1617-1620	4	15
α-helix	1626-1638	13
β-strand	1643-1647	5	15
α-helix	1648-1651	4
β-strand	1660-1663	4	15
β-strand	1667-1670	4	16
β-strand	1675-1678	4	16
α-helix	1679-1680	2
α-helix	1681-1688	8
α-helix	1689-1691	3
β-strand	1700-1706	7	15
α-helix	1711-1718	8
α-helix	1721	1
β-strand	1722	1	14
α-helix	1723	1
α-helix	1732-1741	10
β-strand	1747	1	17
α-helix	1748-1755	8
α-helix	1759-1766	8
α-helix	1768-1771	4
α-helix	1778-1798	21
β-strand	1802-1805	4	17
β-strand	1809-1812	4	17
α-helix	1814-1821	8
α-helix	1826-1835	10
α-helix	1842-1850	9
α-helix	1853-1855	3
α-helix	1864-1872	9
α-helix	1887-1899	13
α-helix	1906-1933	28
β-strand	1935	1	18
α-helix	1937-1951	15
α-helix	1959-1962	4
α-helix	1968-1977	10
α-helix	1983-1986	4
α-helix	1990-1996	7
α-helix	2001-2013	13
β-strand	2017-2023	7	19
β-strand	2030	1	20
β-strand	2034-2043	10	19
α-helix	2046-2047	2
β-strand	2064-2070	7	18
β-strand	2075-2082	8	18
β-strand	2087-2095	9	19
β-strand	2101-2110	10	18
β-strand	2118-2125	8	18
β-strand	2127	1	20

Chain C: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	8	1	18
α-helix	14-18	5
α-helix	21-40	20
α-helix	42-45	4
β-strand	47-48	2	9
α-helix	49-54	6

Chain J: 15 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	2073-2080	8
α-helix	2086-2088	3
β-strand	2090-2092	3	21
α-helix	2093-2094	2
β-strand	2103-2107	5	21
α-helix	2108-2116	9
β-strand	2125-2131	7	21
α-helix	2132-2133	2
β-strand	2139-2146	8	21
β-strand	2150	1	22
β-strand	2151-2152	2	23
β-strand	2157-2158	2	23
α-helix	2163-2164	2
α-helix	2167-2169	3
β-strand	2173-2181	9	21
α-helix	2190-2202	13
β-strand	2212-2217	6	21
β-strand	2223-2230	8	21
α-helix	2232-2240	9
α-helix	2253-2255	3
β-strand	2256-2259	4	21
β-strand	2261-2264	4	21
β-strand	2270-2274	5	21
β-strand	2280	1	22
α-helix	2285-2287	3
β-strand	2296-2298	3	21
α-helix	2300-2303	4
α-helix	2311-2313	3
α-helix	2318-2320	3
α-helix	2323-2326	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
U5 small nuclear ribonucleoprotein 200 kDa helicase	B	protein	1739	Homo sapiens	O75643 (AlphaFold model)
Telomere length and silencing protein 1 homolog	C	protein	293	Homo sapiens	Q9NZ63 (AlphaFold model)
Pre-mRNA-processing-splicing factor 8	J	protein	278	Homo sapiens	Q6P2Q9 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>7OS2_1 U5 small nuclear ribonucleoprotein 200 kDa helicase (chains B)
GAEFDLDQGGEALAPRQVLDLEDLVFTQGSHFMANKRCQLPDGSFRRQRKGYEEVHVPAL
KPKPFGSEEQLLPVEKLPKYAQAGFEGFKTLNRIQSKLYRAALETDENLLLCAPTGAGKT
NVALMCMLREIGKHINMDGTINVDDFKIIYIAPMRSLVQEMVGSFGKRLATYGITVAELT
GDHQLCKEEISATQIIVCTPEKWDIITRKGGERTYTQLVRLIILDEIHLLHDDRGPVLEA
LVARAIRNIEMTQEDVRLIGLSATLPNYEDVATFLRVDPAKGLFYFDNSFRPVPLEQTYV
GITEKKAIKRFQIMNEIVYEKIMEHAGKNQVLVFVHSRKETGKTARAIRDMCLEKDTLGL
FLREGSASTEVLRTEAEQCKNLELKDLLPYGFAIHHAGMTRVDRTLVEDLFADKHIQVLV
STATLAWGVNLPAHTVIIKGTQVYSPEKGRWTELGALDILQMLGRAGRPQYDTKGEGILI
TSHGELQYYLSLLNQQLPIESQMVSKLPDMLNAEIVLGNVQNAKDAVNWLGYAYLYIRML
RSPTLYGISHDDLKGDPLLDQRRLDLVHTAALMLDKNNLVKYDKKTGNFQVTELGRIASH
YYITNDTVQTYNQLLKPTLSEIELFRVFSLSSEFKNITVREEEKLELQKLLERVPIPVKE
SIEEPSAKINVLLQAFISQLKLEGFALMADMVYVTQSAGRLMRAIFEIVLNRGWAQLTDK
TLNLCKMIDKRMWQSMCPLRQFRKLPEEVVKKIEKKNFPFERLYDLNHNEIGELIRMPKM
GKTIHKYVHLFPKLELSVHLQPITRSTLKVELTITPDFQWDEKVHGSSEAFWILVEDVDS
EVILHHEYFLLKAKYAQDEHLITFFVPVFEPLPPQYFIRVVSDRWLSCETQLPVSFRHLI
LPEKYPPPTELLDLQPLPVSALRNSAFESLYQDKFPFFNPIQTQVFNTVYNSDDNVFVGA
PTGSGKTICAEFAILRMLLQSSEGRCVYITPMEALAEQVYMDWYEKFQDRLNKKVVLLTG
ETSTDLKLLGKGNIIISTPEKWDILSRRWKQRKNVQNINLFVVDEVHLIGGENGPVLEVI
CSRMRYISSQIERPIRIVALSSSLSNAKDVAHWLGCSATSTFNFHPNVRPVPLELHIQGF
NISHTQTRLLSMAKPVYHAITKHSPKKPVIVFVPSRKQTRLTAIDILTTCAADIQRQRFL
HCTEKDLIPYLEKLSDSTLKETLLNGVGYLHEGLSPMERRLVEQLFSSGAIQVVVASRSL
CWGMNVAAHLVIIMDTQYYNGKIHAYVDYPIYDVLQMVGHANRPLQDDEGRCVIMCQGSK
KDFFKKFLYEPLPVESHLDHCMHDHFNAEIVTKTIENKQDAVDYLTWTFLYRRMTQNPNY
YNLQGISHRHLSDHLSELVEQTLSDLEQSKCISIEDEMDVAPLNLGMIAAYYYINYTTIE
LFSMSLNAKTKVRGLIEIISNAAEYENIPIRHHEDNLLRQLAQKVPHKLNNPKFNDPHVK
TNLLLQAHLSRMQLSAELQSDTEEILSKAIRLIQACVDVLSSNGWLSPALAAMELAQMVT
QAMWSKDSYLKQLPHFTSEHIKRCTDKGVESVFDIMEMEDEERNALLQLTDSQIADVARF
CNRYPNIELSYEVVDKDSIRSGGPVVVLVQLEREEEVTGPVIAPLFPQKREEGWWVVIGD
AKSNSLISIKRLTLQQKAKVKLDFVAPATGAHNYTLYFMSDAYMGCDQEYKFSVDVKEA

Sequence of entity 2 (C), FASTA

>7OS2_2 Telomere length and silencing protein 1 homolog (chains C)
GAMAMPVVRKIFRRRRGDSESEEDEQDSEEVRLKLEETREVQNLRKRPNGVSAVALLVGE
KVQEETTLVDDPFQMKTGGMVDMKKLKERGKDKISEEEDLHLGTSFSAETNRRDEDADMM
KYIETELKKRKGIVEHEEQKVKPKNAEDCLYELPENIRVSSAKKTEEMLSNQMLSGIPEV
DLGIDAKIKNIISTEDAKARLLAEQQNKKKDSETSFVPTNMAVNYVQHNRFYHEELNAPI
RRNKEEPKARPLRVGDTEKPEPERSPPNRKRPANEKATDDYHYEKFKKMNRRY

Sequence of entity 3 (J), FASTA

>7OS2_3 Pre-mRNA-processing-splicing factor 8 (chains J)
GPLGSMTQTFSSKTEWRVRAISAANLHLRTNHIYVSSDDIKETGYTYILPKNVLKKFICI
SDLRAQIAGYLYGVSPPDNPQVKEIRCIVMVPQWGTHQTVHLPGQLPQHEYLKEMEPLGW
IHTQPNESPQLSPQDVTTHAKIMADNPSWDGEKTIIITCSFTPGSCTLTAYKLTPSGYEW
GRQNTDKGNNPKGYLPSHYERVQMLLSDRFLGFFMVPAQSSWNYNFMGVRHDPNMKYELQ
LANPKEFYHEVHRPSHFLNFALLQEGEVYSADREDLYA

Primary citation

The intrinsically disordered TSSC4 protein acts as a helicase inhibitor, placeholder and multi-interaction coordinator during snRNP assembly and recycling. Bergfort, A., Hilal, T., Kuropka, B. et al. Nucleic Acids Res (2022) 50:2938-2958. DOI 10.1093/nar/gkac087 · PubMed

Other PDB entries of the same protein (UniProt O75643 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2Q0Z 2.0 Å, Crystal structure of Q9P172/Sec63 from Homo sapiens. Northeast Structural Genomics…
8BCE 2.05 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 76
8BC9 2.3 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 24
8BCC 2.35 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 39
8BCB 2.38 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 34
8BC8 2.39 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 18
8BCG 2.39 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 86
6S8Q 2.39 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1
9S2E 2.4 Å, Human intron-lariat spliceosome-Aquarius (ILSaqr)
8BCF 2.42 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and compound 78
7BDK 2.52 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and ADP
7BDJ 2.59 Å, Human Brr2 Helicase Region in complex with C-tail deleted Jab1 and mant-ATPgammaS

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