[English] 日本語
Yorodumi
- PDB-6o16: Crystal structure of murine DHX37 in complex with RNA -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6o16
TitleCrystal structure of murine DHX37 in complex with RNA
Components
  • DEAH (Asp-Glu-Ala-His) box polypeptide 37
  • RNA (5'-R(*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3')
KeywordsHYDROLASE/RNA / RNA helicase / ribosome biogenesis / RNA-dependent ATPase / HYDROLASE-RNA complex
Function / homology
Function and homology information


Major pathway of rRNA processing in the nucleolus and cytosol / positive regulation of male gonad development / U3 snoRNA binding / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosome assembly / helicase activity / brain development / ribosome biogenesis / nuclear membrane / nucleolus ...Major pathway of rRNA processing in the nucleolus and cytosol / positive regulation of male gonad development / U3 snoRNA binding / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ribosome assembly / helicase activity / brain development / ribosome biogenesis / nuclear membrane / nucleolus / RNA binding / ATP binding / cytoplasm
Similarity search - Function
DEAD-box helicase, OB fold / Oligonucleotide/oligosaccharide-binding (OB)-fold / Helicase-associated domain / Helicase associated domain (HA2), winged-helix / Helicase associated domain (HA2) Add an annotation / DEAD/DEAH box helicase / DEAD/DEAH box helicase domain / Helicase conserved C-terminal domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. ...DEAD-box helicase, OB fold / Oligonucleotide/oligosaccharide-binding (OB)-fold / Helicase-associated domain / Helicase associated domain (HA2), winged-helix / Helicase associated domain (HA2) Add an annotation / DEAD/DEAH box helicase / DEAD/DEAH box helicase domain / Helicase conserved C-terminal domain / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
RNA / DEAH (Asp-Glu-Ala-His) box polypeptide 37
Similarity search - Component
Biological speciesMus musculus (house mouse)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.875 Å
AuthorsBoneberg, F. / Brandmann, T. / Kobel, L. / van den Heuvel, J. / Bargsten, K. / Bammert, L. / Kutay, U. / Jinek, M.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Swiss National Science FoundationNCCR RNA & Disease Switzerland
CitationJournal: Rna / Year: 2019
Title: Molecular mechanism of the RNA helicase DHX37 and its activation by UTP14A in ribosome biogenesis.
Authors: Boneberg, F.M. / Brandmann, T. / Kobel, L. / van den Heuvel, J. / Bargsten, K. / Bammert, L. / Kutay, U. / Jinek, M.
History
DepositionFeb 18, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 17, 2019Provider: repository / Type: Initial release
Revision 1.1May 29, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_volume ..._citation.journal_abbrev / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Mar 13, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: DEAH (Asp-Glu-Ala-His) box polypeptide 37
B: DEAH (Asp-Glu-Ala-His) box polypeptide 37
C: RNA (5'-R(*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3')
D: RNA (5'-R(*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3')


Theoretical massNumber of molelcules
Total (without water)223,4644
Polymers223,4644
Non-polymers00
Water0
1
A: DEAH (Asp-Glu-Ala-His) box polypeptide 37
C: RNA (5'-R(*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3')


Theoretical massNumber of molelcules
Total (without water)111,7322
Polymers111,7322
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3240 Å2
ΔGint-34 kcal/mol
Surface area38440 Å2
MethodPISA
2
B: DEAH (Asp-Glu-Ala-His) box polypeptide 37
D: RNA (5'-R(*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3')


Theoretical massNumber of molelcules
Total (without water)111,7322
Polymers111,7322
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3160 Å2
ΔGint-31 kcal/mol
Surface area38470 Å2
MethodPISA
Unit cell
Length a, b, c (Å)83.829, 137.593, 94.225
Angle α, β, γ (deg.)90.00, 93.34, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein DEAH (Asp-Glu-Ala-His) box polypeptide 37


Mass: 108715.477 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Dhx37
Production host: Spodoptera aff. frugiperda 2 RZ-2014 (butterflies/moths)
References: UniProt: Q6NZL1
#2: RNA chain RNA (5'-R(*UP*UP*UP*UP*UP*UP*UP*UP*UP*U)-3')


Mass: 3016.700 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.65 Å3/Da / Density % sol: 53.57 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 0.1 M Bis-Tris propane pH 7.0, 0.2 M NaNO3, 15% (w/v) polyethylene glycol (PEG)

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.0077 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Aug 26, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0077 Å / Relative weight: 1
ReflectionResolution: 2.875→47.032 Å / Num. obs: 93431 / % possible obs: 97.88 % / Redundancy: 3.4 % / Biso Wilson estimate: 64.06 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.1026 / Rpim(I) all: 0.06542 / Rrim(I) all: 0.122 / Net I/σ(I): 9.76
Reflection shellResolution: 2.8875→2.98 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.625 / Mean I/σ(I) obs: 1.57 / Num. unique obs: 4209 / CC1/2: 0.872 / Rpim(I) all: 0.4113 / Rrim(I) all: 0.7505 / % possible all: 86.19

-
Processing

Software
NameVersionClassification
PHENIX(1.14_3260)refinement
XDSdata reduction
XDSdata scaling
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 2.875→47.032 Å / SU ML: 0.53 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 33.04 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2948 4684 5.02 %
Rwork0.2703 --
obs0.2715 93377 97.69 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.875→47.032 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12605 394 0 0 12999
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00513321
X-RAY DIFFRACTIONf_angle_d0.79218142
X-RAY DIFFRACTIONf_dihedral_angle_d16.7378147
X-RAY DIFFRACTIONf_chiral_restr0.1222089
X-RAY DIFFRACTIONf_plane_restr0.0062242
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.875-2.90760.5226840.4611545X-RAY DIFFRACTION52
2.9076-2.94180.38221570.36573074X-RAY DIFFRACTION100
2.9418-2.97770.37351650.36053000X-RAY DIFFRACTION100
2.9777-3.01540.36961600.34933004X-RAY DIFFRACTION100
3.0154-3.05510.36421560.34643071X-RAY DIFFRACTION100
3.0551-3.09690.35331590.35063021X-RAY DIFFRACTION100
3.0969-3.14120.36631540.32213018X-RAY DIFFRACTION100
3.1412-3.1880.38761730.33012994X-RAY DIFFRACTION100
3.188-3.23780.38651450.33453076X-RAY DIFFRACTION100
3.2378-3.29090.37041700.31143014X-RAY DIFFRACTION100
3.2909-3.34760.35471650.3083031X-RAY DIFFRACTION100
3.3476-3.40850.36221430.30422967X-RAY DIFFRACTION99
3.4085-3.4740.39361670.30733001X-RAY DIFFRACTION99
3.474-3.54490.37031490.30273028X-RAY DIFFRACTION100
3.5449-3.6220.31751710.29633034X-RAY DIFFRACTION99
3.622-3.70620.31731470.28493006X-RAY DIFFRACTION99
3.7062-3.79880.31951590.27553007X-RAY DIFFRACTION99
3.7988-3.90150.30171590.26472945X-RAY DIFFRACTION99
3.9015-4.01620.3011590.27063035X-RAY DIFFRACTION98
4.0162-4.14580.26141540.25892953X-RAY DIFFRACTION98
4.1458-4.29390.2931650.25152969X-RAY DIFFRACTION98
4.2939-4.46570.23141530.25152963X-RAY DIFFRACTION98
4.4657-4.66870.31371600.24142957X-RAY DIFFRACTION98
4.6687-4.91460.23581590.23943020X-RAY DIFFRACTION99
4.9146-5.22220.27171580.24233002X-RAY DIFFRACTION99
5.2222-5.62480.26041570.26372981X-RAY DIFFRACTION99
5.6248-6.18970.25451580.24893013X-RAY DIFFRACTION99
6.1897-7.08280.28441630.26052974X-RAY DIFFRACTION99
7.0828-8.91360.20731590.21682971X-RAY DIFFRACTION98
8.9136-47.03870.21431560.21823019X-RAY DIFFRACTION99
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.727-0.10220.16491.8159-0.34370.85510.0084-0.1285-0.0680.2960.03760.4740.317-0.0764-0.00340.5616-0.03210.10140.3985-0.0040.4037-29.142911.905-48.1323
20.44170.6680.42171.55040.09180.8712-0.0983-0.19040.08980.47530.0351-0.0101-0.07850.0163-00.47830.0822-0.0310.4480.0220.3969-18.890336.8493-47.6694
30.7070.6283-1.5510.1024-0.4827-0.04110.40.22840.02850.4391-0.1363-0.06681.34350.70690-3.2743-1.4481-0.1452-0.4745-0.07710.30482.307647.7904-62.3466
40.6736-0.10920.00210.7384-0.32470.38860.02090.17190.1203-0.3464-0.04310.16960.1406-0.079600.9858-0.0536-0.00560.5520.03140.4891-21.180236.9506-4.423
50.6594-0.1097-0.55941.273-0.02470.45260.09320.18560.0345-0.2714-0.12280.5441-0.1698-0.303200.53240.0969-0.0850.6364-0.00460.6262-41.760120.15522.04
61.29040.3088-0.04661.69130.02120.86930.10040.1038-0.1227-0.1014-0.0509-0.0087-0.0277-0.01610.01460.2801-0.01910.05290.2499-0.02940.1951-18.92371.3484-4.7257
70.1941-0.50260.74460.3397-0.59461.08940.0792-0.1013-0.03240.0336-0.1145-0.17120.0320.103900.4948-0.01480.01990.49940.0360.58982.0333-6.121217.7228
80.02450.10920.01710.05050.04930.0314-0.09-0.16790.12770.05990.0872-0.11710.3843-0.10300.64910.0886-0.02290.626-0.00930.6197-31.409834.3702-52.4956
90.0394-0.1266-0.03720.06270.064-0.0607-0.1793-0.4815-0.1706-0.28330.2371-0.0358-0.9147-0.325700.5122-0.0433-0.05340.7670.1010.7186-33.65986.26491.6582
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 231 through 707 )
2X-RAY DIFFRACTION2chain 'A' and (resid 708 through 895 )
3X-RAY DIFFRACTION3chain 'A' and (resid 896 through 1149 )
4X-RAY DIFFRACTION4chain 'B' and (resid 231 through 423 )
5X-RAY DIFFRACTION5chain 'B' and (resid 424 through 736 )
6X-RAY DIFFRACTION6chain 'B' and (resid 737 through 925 )
7X-RAY DIFFRACTION7chain 'B' and (resid 926 through 1148 )
8X-RAY DIFFRACTION8chain 'C' and (resid 1 through 10 )
9X-RAY DIFFRACTION9chain 'D' and (resid 1 through 10 )

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more