[English] 日本語
Yorodumi
- PDB-2j7n: Structure of the RNAi polymerase from Neurospora crassa -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2j7n
TitleStructure of the RNAi polymerase from Neurospora crassa
ComponentsRNA-DEPENDENT RNA POLYMERASE
KeywordsHYDROLASE / RNAI RESPONSE / RNA-DIRECTED RNA POLYMERASE
Function / homology
Function and homology information


nuclear RNA-directed RNA polymerase complex / siRNA processing / RNA-directed RNA polymerase / RNA-dependent RNA polymerase activity / GTP binding / RNA binding / ATP binding / identical protein binding / metal ion binding
Similarity search - Function
RNA-dependent RNA polymerase, slab domain, helical subdomain-like / RNA-dependent RNA polymerase, eukaryotic-type / RNA dependent RNA polymerase / Helicase, Ruva Protein; domain 3 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
RNA-dependent RNA polymerase
Similarity search - Component
Biological speciesNEUROSPORA CRASSA (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.3 Å
AuthorsSalgado, P.S. / Koivunen, M.R.L. / Makeyev, E.V. / Bamford, D.H. / Stuart, D.I. / Grimes, J.M.
Citation
Journal: Plos Biol. / Year: 2006
Title: The Structure of an Rnai Polymerase Links RNA Silencing and Transcription.
Authors: Salgado, P.S. / Koivunen, M.R.L. / Makeyev, E.V. / Bamford, D.H. / Stuart, D.I. / Grimes, J.M.
#1: Journal: Mol.Cell / Year: 2002
Title: Cellular RNA-Dependent RNA Polymerase Involved in Posttranscriptional Gene Silencing Has Two Distinct Activity Modes.
Authors: Makeyev, E.V. / Bamford, D.H.
History
DepositionOct 13, 2006Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 13, 2006Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Refinement description / Version format compliance
Revision 1.2Jul 5, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3May 8, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO ... SHEET DETERMINATION METHOD: DSSP THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. THE SHEETS PRESENTED AS "AE" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "BE" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: RNA-DEPENDENT RNA POLYMERASE
B: RNA-DEPENDENT RNA POLYMERASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)233,5595
Polymers233,4182
Non-polymers1413
Water16,574920
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9370 Å2
ΔGint-68.4 kcal/mol
Surface area80930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)101.021, 122.553, 114.701
Angle α, β, γ (deg.)90.00, 108.90, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22B
13A
23B
14A
24B
15A
25B
16A
26B

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLUGLULYSLYS2AA470 - 64690 - 266
211GLUGLULYSLYS2BB470 - 64690 - 266
112VALVALARGARG2AA647 - 807267 - 427
212VALVALARGARG2BB647 - 807267 - 427
122VALVALHISHIS2AA914 - 1161534 - 781
222VALVALHISHIS2BB914 - 1161534 - 781
113ARGARGGLNGLN2AA837 - 888457 - 508
213ARGARGGLNGLN2BB837 - 888457 - 508
123ALAALAGLYGLY2AA1196 - 1372816 - 992
223ALAALAGLYGLY2BB1196 - 1372816 - 992
114ASPASPASNASN4AA808 - 836428 - 456
214ASPASPASNASN4BB808 - 836428 - 456
115LYSLYSARGARG4AA887 - 913507 - 533
215LYSLYSARGARG4BB887 - 913507 - 533
116ILEILEGLYGLY4AA1162 - 1195782 - 815
216ILEILEGLYGLY4BB1162 - 1195782 - 815

NCS ensembles :
ID
1
2
3
4
5
6

-
Components

#1: Protein RNA-DEPENDENT RNA POLYMERASE / HYPOTHETICAL PROTEIN NCU07534.1


Mass: 116708.938 Da / Num. of mol.: 2 / Fragment: RESIDUES 381-1402
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) NEUROSPORA CRASSA (fungus) / Plasmid: PEM69 / Production host: SACCHAROMYCES CEREVISIAE (brewer's yeast) / Strain (production host): INVSC1 / References: UniProt: Q9Y7G6
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 920 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.01 Å3/Da / Density % sol: 58.8 %
Crystal growDetails: 100 MM TRISHCL PH 7.5, 150 MM NACL, 8% PEG 6000, AND 5 MM MGCL2.

-
Data collection

Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 1
DetectorType: MARRESEARCH / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.3→20 Å / Num. obs: 114252 / % possible obs: 97.9 % / Observed criterion σ(I): 0 / Redundancy: 15.3 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 18.2
Reflection shellResolution: 2.3→2.38 Å / Mean I/σ(I) obs: 1.3 / % possible all: 100

-
Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
SnBphasing
SOLVEphasing
REFMAC5.2.0005refinement
RefinementMethod to determine structure: MAD / Resolution: 2.3→19.98 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.925 / SU B: 14.819 / SU ML: 0.193 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.306 / ESU R Free: 0.239 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. A DIMER IS PRESENT IN THE ASYMMETRIC UNIT. HOWEVER EACH MONOMER HAS A NUMBER OF DOMAINS THAT ARE RELATED TO THEIR DIMERIC PARTNERS BY ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. A DIMER IS PRESENT IN THE ASYMMETRIC UNIT. HOWEVER EACH MONOMER HAS A NUMBER OF DOMAINS THAT ARE RELATED TO THEIR DIMERIC PARTNERS BY SLIGHTLY DIFFERENT NCS SYMMETRY RELATIONSHIPS.
RfactorNum. reflection% reflectionSelection details
Rfree0.264 5748 5 %RANDOM
Rwork0.217 ---
obs0.219 108414 97.7 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 51.92 Å2
Baniso -1Baniso -2Baniso -3
1-0.03 Å20 Å2-0.09 Å2
2--0.55 Å20 Å2
3----0.63 Å2
Refinement stepCycle: LAST / Resolution: 2.3→19.98 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15018 0 7 920 15945
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.02215406
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.5241.95520850
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg9.06351855
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.66523.38716
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.02152684
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.13615116
X-RAY DIFFRACTIONr_chiral_restr0.1090.22233
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0211707
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2710.37930
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3280.510386
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.230.51487
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2510.372
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.3930.523
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.5681.59523
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.966215057
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.3436694
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it2.0854.55793
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A584tight positional0.080.05
12B584tight positional0.080.05
21A1636tight positional0.090.05
22B1636tight positional0.090.05
31A828tight positional0.070.05
32B828tight positional0.070.05
11A572medium positional0.460.3
12B572medium positional0.460.3
21A1604medium positional0.430.3
22B1604medium positional0.430.3
31A871medium positional0.420.3
32B871medium positional0.420.3
41A241medium positional0.430.3
42B241medium positional0.430.3
51A233medium positional0.820.3
52B233medium positional0.820.3
61A268medium positional0.530.3
62B268medium positional0.530.3
11A584tight thermal0.95
12B584tight thermal0.95
21A1636tight thermal1.455
22B1636tight thermal1.455
31A828tight thermal0.885
32B828tight thermal0.885
11A572medium thermal1.157
12B572medium thermal1.157
21A1604medium thermal1.697
22B1604medium thermal1.697
31A871medium thermal1.197
32B871medium thermal1.197
41A241medium thermal1.527
42B241medium thermal1.527
51A233medium thermal1.427
52B233medium thermal1.427
61A268medium thermal0.877
62B268medium thermal0.877
LS refinement shellResolution: 2.3→2.36 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.355 455
Rwork0.305 7801
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)
13.05090.99320.05255.3654-0.18622.36650.07560.27290.9239-0.04140.08790.8921-0.5755-0.4857-0.16350.10340.16020.0091-0.10850.1490.256646.96385.120847.7432
21.4366-0.0001-0.59430.48980.06321.45310.0730.0434-0.0048-0.0944-0.05950.07250.1103-0.1785-0.0136-0.17910.0107-0.0231-0.2834-0.0104-0.172251.837756.764367.2763
33.1055-0.4905-0.59833.165-0.96055.78410.02710.22010.14170.23020.09870.3586-0.6385-1.4584-0.1258-0.11040.15420.0640.09760.0027-0.200661.4774104.184782.6035
48.231814.03990.411424.24650.96920.6860.240.061-0.00320.2116-0.0113-0.2319-0.31760.154-0.2287-0.0276-0.06270.0708-0.0595-0.0334-0.139451.737671.258896.9307
54.092111.9630.312734.97340.91420.0239-0.06430.13160.6172-0.2992-0.03611.8304-0.170.16960.10040.1188-0.02130.00310.1983-0.0170.084249.686283.682288.7772
610.074510.22576.761521.137510.970811.77-0.3015-0.76181.14480.0251-0.31080.1323-1.57320.23730.61220.1007-0.09680.00730.0948-0.05910.141945.814583.180398.9139
74.94931.2770.2887.31660.07093.75090.0587-0.30241.42410.06680.0577-0.3456-1.58770.7228-0.11640.6045-0.36620.14670.3365-0.36460.448100.172485.1662119.8034
82.42550.2835-0.71830.5677-0.12232.28860.1706-0.3190.12170.062-0.0362-0.0701-0.0120.2445-0.1344-0.2055-0.0309-0.0267-0.2741-0.0164-0.159996.806257.310798.7019
92.19540.5102-0.36972.7835-0.9775.4472-0.01030.03090.17150.1998-0.1377-0.3693-0.64450.45270.1481-0.0898-0.04560.0051-0.25260.0231-0.136282.965106.247177.9687
1014.6637-21.02112.14630.1408-3.04270.50070.6165-0.15070.3233-1.0158-0.0692-0.04620.0398-0.2486-0.54730.06260.06250.1234-0.12210.02150.03796.478671.978167.3835
1110.0526-14.29410.993621.2878-1.69470.18070.06950.22090.34740.0741-0.459-1.2530.04030.33530.38950.08710.0928-0.0420.07160.00080.131997.390187.110873.6408
128.8983-12.6638.128836.2595-20.779217.18420.0150.88740.9819-0.5206-0.13210.2734-1.2232-0.20960.11710.16490.07490.0360.09990.05420.2518102.332884.247464.8229
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A390 - 646
2X-RAY DIFFRACTION2A647 - 807
3X-RAY DIFFRACTION2A914 - 1161
4X-RAY DIFFRACTION3A837 - 888
5X-RAY DIFFRACTION3A1196 - 1372
6X-RAY DIFFRACTION4A808 - 836
7X-RAY DIFFRACTION5A889 - 913
8X-RAY DIFFRACTION6A1162 - 1195
9X-RAY DIFFRACTION7B390 - 646
10X-RAY DIFFRACTION8B647 - 807
11X-RAY DIFFRACTION8B914 - 1161
12X-RAY DIFFRACTION9B837 - 888
13X-RAY DIFFRACTION9B1196 - 1372
14X-RAY DIFFRACTION10B808 - 836
15X-RAY DIFFRACTION11B889 - 913
16X-RAY DIFFRACTION12B1162 - 1195

+
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://pdbjlvh1.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