[English] 日本語
Yorodumi
- PDB-4qu4: Improved refinement of the Mtr4 apo crystal structure -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4qu4
TitleImproved refinement of the Mtr4 apo crystal structure
ComponentsATP-dependent RNA helicase DOB1
KeywordsHYDROLASE / rec-A FOLD / winged-helix-turn-helix / antiparallel-coiled-coil / DSHCT domain / helicase / nucleotide binding / phosphoprotein / rRNA processing / TRAMP / ATP binding / nucleus
Function / homology
Function and homology information


nuclear mRNA surveillance of mRNA 3'-end processing / TRAMP complex / nuclear polyadenylation-dependent mRNA catabolic process / U5 snRNA 3'-end processing / TRAMP-dependent tRNA surveillance pathway / RNA fragment catabolic process / U4 snRNA 3'-end processing / nuclear polyadenylation-dependent rRNA catabolic process / poly(A)-dependent snoRNA 3'-end processing / exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) ...nuclear mRNA surveillance of mRNA 3'-end processing / TRAMP complex / nuclear polyadenylation-dependent mRNA catabolic process / U5 snRNA 3'-end processing / TRAMP-dependent tRNA surveillance pathway / RNA fragment catabolic process / U4 snRNA 3'-end processing / nuclear polyadenylation-dependent rRNA catabolic process / poly(A)-dependent snoRNA 3'-end processing / exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / 3'-5' RNA helicase activity / rRNA catabolic process / nuclear mRNA surveillance / poly(A) binding / RNA catabolic process / maturation of 5.8S rRNA / Major pathway of rRNA processing in the nucleolus and cytosol / mRNA processing / RNA helicase activity / oxidoreductase activity / RNA helicase / mRNA binding / nucleolus / ATP hydrolysis activity / DNA binding / ATP binding / nucleus
Similarity search - Function
Elongation Factor Tu (Ef-tu); domain 3 - #300 / YheA-like fold - #20 / YheA-like fold / Sec63 N-terminal domain-like fold - #30 / Sec63 N-terminal domain-like fold / rRNA-processing arch domain / Mtr4-like, beta-barrel domain / : / Exosome RNA helicase MTR4-like, stalk / ATP-dependent RNA helicase Ski2, C-terminal ...Elongation Factor Tu (Ef-tu); domain 3 - #300 / YheA-like fold - #20 / YheA-like fold / Sec63 N-terminal domain-like fold - #30 / Sec63 N-terminal domain-like fold / rRNA-processing arch domain / Mtr4-like, beta-barrel domain / : / Exosome RNA helicase MTR4-like, stalk / ATP-dependent RNA helicase Ski2, C-terminal / ATP-dependent RNA helicase Ski2-like / DSHCT (NUC185) domain / DSHCT / Prismane-like superfamily / DEAD/DEAH box helicase / DEAD/DEAH box helicase domain / Elongation Factor Tu (Ef-tu); domain 3 / 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 nucleotide triphosphate hydrolases / Up-down Bundle / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHOSPHATE ION / ATP-dependent RNA helicase DOB1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3.392 Å
AuthorsJohnson, S.J. / Taylor, L.L.
Citation
Journal: Nucleic Acids Res. / Year: 2014
Title: The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding.
Authors: Taylor, L.L. / Jackson, R.N. / Rexhepaj, M. / King, A.K. / Lott, L.K. / van Hoof, A. / Johnson, S.J.
#1: Journal: Embo J. / Year: 2010
Title: The crystal structure of MTR4 reveals a novel arch domain required for rRNA processing.
Authors: Jackson, R.N. / Klauer, A.A. / Hintze, B.J. / Robinson, H. / van Hoof, A. / Johnson, S.J.
History
DepositionJul 10, 2014Deposition site: RCSB / Processing site: RCSB
SupersessionDec 3, 2014ID: 3L9O
Revision 1.0Dec 3, 2014Provider: repository / Type: Initial release
Revision 1.1Jan 14, 2015Group: Database references
Revision 1.2Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: ATP-dependent RNA helicase DOB1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)126,5794
Polymers126,2941
Non-polymers2853
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)133.516, 133.516, 190.949
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121

-
Components

#1: Protein ATP-dependent RNA helicase DOB1 / mRNA transport regulator MTR4


Mass: 126294.484 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: DOB1, J1158, MTR4, MTR4/YJL050W, YJL050W / Plasmid: pET151 Directional TOPO / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21-CodonPlus(DE3)-RIL / References: UniProt: P47047, RNA helicase
#2: Chemical ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: PO4

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.89 Å3/Da / Density % sol: 68.38 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 2.4 M ammonium dihydrogen phosphate, 0.1 M Tris, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K

-
Data collection

DiffractionMean temperature: 190 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 0.9793 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jan 19, 2008
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 3.389→30 Å / Num. all: 26177 / Num. obs: 26177 / % possible obs: 94 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 10 % / Biso Wilson estimate: 137.4 Å2
Reflection shellResolution: 3.389→3.52 Å / Redundancy: 5.8 % / Mean I/σ(I) obs: 1.9 / Rsym value: 0.494 / % possible all: 59.9

-
Processing

Software
NameVersionClassification
ADSCQuantumdata collection
SOLVEphasing
PHENIX(phenix.refine: 1.9_1692)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: SAD / Resolution: 3.392→28.757 Å / SU ML: 0.53 / σ(F): 1.34 / Phase error: 38.78 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2991 1268 4.86 %
Rwork0.2475 --
obs0.2502 26095 93.82 %
all-26095 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 164.45 Å2
Refinement stepCycle: LAST / Resolution: 3.392→28.757 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6665 0 15 0 6680
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.016789
X-RAY DIFFRACTIONf_angle_d1.4639265
X-RAY DIFFRACTIONf_dihedral_angle_d14.9522290
X-RAY DIFFRACTIONf_chiral_restr0.0521123
X-RAY DIFFRACTIONf_plane_restr0.0071196
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.392-3.52780.3918960.35391746X-RAY DIFFRACTION60
3.5278-3.68810.42551230.34232464X-RAY DIFFRACTION85
3.6881-3.88210.38331540.32062881X-RAY DIFFRACTION99
3.8821-4.12460.31671370.2932888X-RAY DIFFRACTION100
4.1246-4.4420.30431380.24852943X-RAY DIFFRACTION100
4.442-4.88710.29871490.22192913X-RAY DIFFRACTION100
4.8871-5.58980.33051430.25192951X-RAY DIFFRACTION100
5.5898-7.02550.33681550.31242973X-RAY DIFFRACTION100
7.0255-28.75830.24991730.19833068X-RAY DIFFRACTION100
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)
11.4901-1.06261.51180.7245-1.03921.477-0.4911-0.53640.54640.83970.5707-1.08940.88780.6098-01.4882-0.57180.26471.6363-0.37161.8414121.405354.191481.9824
23.94612.79573.18364.4006-0.7886.6049-0.0764-0.49190.77720.0887-0.41640.34070.277-0.3368-0.00010.8181-0.13930.26571.1179-0.30271.4826117.508651.830255.8376
32.66380.7969-1.44615.41081.61213.2597-0.0921-0.73130.6103-0.66950.8091-0.7377-0.28630.6662-01.5352-0.35860.10141.5788-0.31721.3137101.934964.183787.3387
42.22770.1277-0.08080.74230.1021.49460.1456-0.19490.3534-1.9922-0.59730.0948-2.5728-0.9086-0.14194.98420.0373-0.22471.015-0.01511.66595.373279.665666.3684
51.09020.25291.23923.39274.62786.2213-0.63960.29960.2742-1.52290.6201-0.0506-1.43090.378-0.00041.8011-0.4140.16731.5463-0.18931.4673100.15655.545271.3988
61.04271.7733-0.83132.6099-1.55781.779-0.3803-0.8651-0.5577-0.52510.003-0.73330.19240.9719-01.59430.04250.2551.79750.06881.546390.496622.556770.4676
75.52181.64661.8743.07450.67173.89790.3039-0.5016-0.10940.37160.01910.06220.490.4328-01.38070.35540.02931.5862-0.07461.436471.454344.533182.5487
81.4806-1.1511-0.77193.55860.15842.1061-0.0988-0.53610.0787-0.15490.02810.3412-0.25930.322801.6927-0.00180.07561.51410.17651.534572.657725.587583.1105
90.8322-0.75010.20442.2311-0.2693-0.0238-0.58770.16230.0311-1.64560.1161.1313-0.749-0.6646-0.00012.3586-0.1513-0.21262.3193-0.05161.879982.71746.199843.0707
101.0882-0.1273-0.52640.03940.21210.5071-0.4152-0.20020.69480.279-0.67910.0441-1.0321-0.923-0.0183.54750.3674-0.20592.53580.21041.53585.907567.173145.1656
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 79:122)
2X-RAY DIFFRACTION2(chain A and resid 123:321)
3X-RAY DIFFRACTION3(chain A and resid 322:415)
4X-RAY DIFFRACTION4(chain A and resid 416:496)
5X-RAY DIFFRACTION5(chain A and resid 497:599)
6X-RAY DIFFRACTION6(chain A and resid 600:661)
7X-RAY DIFFRACTION7(chain A and resid 662:780)
8X-RAY DIFFRACTION8(chain A and resid 781:877)
9X-RAY DIFFRACTION9(chain A and resid 878:995)
10X-RAY DIFFRACTION10(chain A and resid 996:1072)

+
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