[English] 日本語
Yorodumi
- PDB-3nfi: Crystal structure of tandem winged helix domain of RNA polymerase... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3nfi
TitleCrystal structure of tandem winged helix domain of RNA polymerase I subunit A49
ComponentsDNA-directed RNA polymerase I subunit RPA49Polymerase
KeywordsDNA BINDING PROTEIN / TRANSCRIPTION / winged helix / RNA polymerase / DNA binding
Function / homology
Function and homology information


RNA polymerase I preinitiation complex assembly / RNA Polymerase I Transcription Initiation / regulation of cell size / RNA Polymerase I Promoter Escape / RNA polymerase I activity / termination of RNA polymerase I transcription / nucleolar large rRNA transcription by RNA polymerase I / transcription initiation at RNA polymerase I promoter / transcription elongation by RNA polymerase I / RNA polymerase I complex ...RNA polymerase I preinitiation complex assembly / RNA Polymerase I Transcription Initiation / regulation of cell size / RNA Polymerase I Promoter Escape / RNA polymerase I activity / termination of RNA polymerase I transcription / nucleolar large rRNA transcription by RNA polymerase I / transcription initiation at RNA polymerase I promoter / transcription elongation by RNA polymerase I / RNA polymerase I complex / transcription by RNA polymerase I / ribosome biogenesis / nucleolus / DNA binding / nucleus
Similarity search - Function
RNA polymerase I associated factor, A49-like / A49-like RNA polymerase I associated factor
Similarity search - Domain/homology
DNA-directed RNA polymerase I subunit RPA49
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.9 Å
AuthorsGeiger, S.R. / Lorenzen, K. / Schreieck, A. / Hanecker, P. / Kostrewa, D. / Heck, A.J.R. / Cramer, P.
CitationJournal: Mol.Cell / Year: 2010
Title: RNA Polymerase I Contains a TFIIF-Related DNA-Binding Subcomplex.
Authors: Geiger, S.R. / Lorenzen, K. / Schreieck, A. / Hanecker, P. / Kostrewa, D. / Heck, A.J. / Cramer, P.
History
DepositionJun 10, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 8, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Mar 25, 2015Group: Atomic model / Database references

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: DNA-directed RNA polymerase I subunit RPA49
B: DNA-directed RNA polymerase I subunit RPA49
C: DNA-directed RNA polymerase I subunit RPA49
D: DNA-directed RNA polymerase I subunit RPA49
E: DNA-directed RNA polymerase I subunit RPA49
hetero molecules


Theoretical massNumber of molelcules
Total (without water)136,0636
Polymers135,7095
Non-polymers3541
Water14,160786
1
A: DNA-directed RNA polymerase I subunit RPA49


Theoretical massNumber of molelcules
Total (without water)27,1421
Polymers27,1421
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: DNA-directed RNA polymerase I subunit RPA49


Theoretical massNumber of molelcules
Total (without water)27,1421
Polymers27,1421
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: DNA-directed RNA polymerase I subunit RPA49


Theoretical massNumber of molelcules
Total (without water)27,1421
Polymers27,1421
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: DNA-directed RNA polymerase I subunit RPA49


Theoretical massNumber of molelcules
Total (without water)27,1421
Polymers27,1421
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
5
E: DNA-directed RNA polymerase I subunit RPA49
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,4962
Polymers27,1421
Non-polymers3541
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)85.110, 78.100, 100.670
Angle α, β, γ (deg.)90.00, 113.39, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein
DNA-directed RNA polymerase I subunit RPA49 / Polymerase / A49 / DNA-directed RNA polymerase I 49 kDa polypeptide


Mass: 27141.715 Da / Num. of mol.: 5 / Fragment: UNP residues 171-403 / Mutation: L178M, L261M
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: N0880, RPA49, RRN13, YNL248C / Plasmid: pET28b / Production host: Escherichia coli (E. coli) / Strain (production host): BL 21 (DE) RIL / References: UniProt: Q01080, DNA-directed RNA polymerase
#2: Chemical ChemComp-PE4 / 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL / POLYETHYLENE GLYCOL PEG4000 / Polyethylene glycol


Mass: 354.436 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C16H34O8 / Comment: precipitant*YM
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 786 / Source method: isolated from a natural source / Formula: H2O
Nonpolymer detailsPE4 E 1 IS PEG 4000 fragment

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.29 Å3/Da / Density % sol: 46.21 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 24% PEG 3350, 50 mM Tris pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

-
Data collection

DiffractionMean temperature: 70 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9790, 0.9790, 0.9180
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: May 1, 2009 / Details: torodial focusing mirror
RadiationMonochromator: channel cut ESRF monochromator / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.9791
20.9181
ReflectionResolution: 1.9→80 Å / Num. all: 95580 / Num. obs: 94313 / % possible obs: 97.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Biso Wilson estimate: 31.04 Å2 / Rmerge(I) obs: 0.066 / Rsym value: 0.066 / Net I/σ(I): 14.78
Reflection shellResolution: 1.9→2.08 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.606 / Mean I/σ(I) obs: 3.4 / Rsym value: 0.606 / % possible all: 99.8

-
Processing

Software
NameVersionClassification
ADSCQuantumdata collection
SHARPphasing
BUSTER2.9.2refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: MAD / Resolution: 1.9→27.82 Å / Cor.coef. Fo:Fc: 0.9527 / Cor.coef. Fo:Fc free: 0.9345 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.2235 4711 5 %RANDOM
Rwork0.1886 ---
obs0.1903 94199 --
all-94199 --
Displacement parametersBiso mean: 40.4 Å2
Baniso -1Baniso -2Baniso -3
1-1.0977 Å20 Å2-2.3971 Å2
2---0.0066 Å20 Å2
3----1.0911 Å2
Refine analyzeLuzzati coordinate error obs: 0.262 Å
Refinement stepCycle: LAST / Resolution: 1.9→27.82 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8717 0 12 786 9515
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.019109HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.0412379HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d3334SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes228HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1301HARMONIC5
X-RAY DIFFRACTIONt_it9109HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion2.74
X-RAY DIFFRACTIONt_other_torsion15.85
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact
LS refinement shellResolution: 1.9→1.95 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2554 309 4.84 %
Rwork0.2444 6079 -
all0.2449 6388 -
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)
10.36520.02530.04980.7259-0.36181.1862-0.02650.00160.01730.02880.03370.0147-0.0323-0.1177-0.0072-0.01780.0039-0.0331-0.0227-0.0031-0.05831.120614.462242.8828
24.3712-0.79241.29450.5255-0.06791.24880.03340.1043-0.2632-0.03150.00480.07720.0593-0.0564-0.0382-0.05340.0023-0.0487-0.13880.0223-0.124558.7738-0.372162.6149
32.3741-0.55910.7840.9493-0.16571.59710.1329-0.1008-0.24720.07860.02990.06110.0505-0.1383-0.1628-0.1114-0.0473-0.0352-0.08060.026-0.041135.187243.181377.5871
41.08680.20270.12071.3205-0.19290.9810.01080.0034-0.09310.0761-0.03420.0158-0.015-0.0370.0233-0.05360.0191-0.0107-0.0536-0.0029-0.065570.337349.010281.7861
51.16620.31890.37361.06460.09531.3009-0.10820.06520.1013-0.10990.02530.0432-0.22980.06740.0829-0.0035-0.0255-0.0489-0.07990.0181-0.083888.027416.646373.852
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{A|*}A185 - 403
2X-RAY DIFFRACTION2{B|*}B172 - 403
3X-RAY DIFFRACTION3{C|*}C184 - 403
4X-RAY DIFFRACTION4{D|*}D184 - 403
5X-RAY DIFFRACTION5{E|*}E184 - 403

+
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