[English] 日本語
Yorodumi
- PDB-4b8b: N-Terminal domain of the yeast Not1 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4b8b
TitleN-Terminal domain of the yeast Not1
ComponentsGENERAL NEGATIVE REGULATOR OF TRANSCRIPTION SUBUNIT 1
KeywordsTRANSCRIPTION
Function / homology
Function and homology information


response to pheromone triggering conjugation with cellular fusion / negative regulation of cytoplasmic mRNA processing body assembly / pseudohyphal growth / CCR4-NOT core complex / nuclear-transcribed mRNA poly(A) tail shortening / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / ATPase activator activity / P-body / transcription elongation by RNA polymerase II / positive regulation of transcription elongation by RNA polymerase II ...response to pheromone triggering conjugation with cellular fusion / negative regulation of cytoplasmic mRNA processing body assembly / pseudohyphal growth / CCR4-NOT core complex / nuclear-transcribed mRNA poly(A) tail shortening / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / ATPase activator activity / P-body / transcription elongation by RNA polymerase II / positive regulation of transcription elongation by RNA polymerase II / negative regulation of translation / molecular adaptor activity / regulation of cell cycle / regulation of transcription by RNA polymerase II / nucleus / cytoplasm
Similarity search - Function
CCR4-NOT transcription complex subunit 1, HEAT repeat 1 / CCR4-NOT transcription complex subunit 1 HEAT repeat / CCR4-Not complex component, Not1, C-terminal / CCR4-NOT transcription complex subunit 1, domain 4 / CCR4-NOT transcription complex subunit 1, CAF1-binding domain / CCR4-NOT transcription complex subunit 1, TTP binding domain / CCR4-NOT transcription complex subunit 1, HEAT repeat / CCR4-NOT subunit 1, TTP binding domain superfamily / CCR4-NOT transcription complex subunit 1 / CCR4-Not complex component, Not1 ...CCR4-NOT transcription complex subunit 1, HEAT repeat 1 / CCR4-NOT transcription complex subunit 1 HEAT repeat / CCR4-Not complex component, Not1, C-terminal / CCR4-NOT transcription complex subunit 1, domain 4 / CCR4-NOT transcription complex subunit 1, CAF1-binding domain / CCR4-NOT transcription complex subunit 1, TTP binding domain / CCR4-NOT transcription complex subunit 1, HEAT repeat / CCR4-NOT subunit 1, TTP binding domain superfamily / CCR4-NOT transcription complex subunit 1 / CCR4-Not complex component, Not1 / CCR4-Not complex, Not1 subunit, domain of unknown function DUF3819 / CCR4-NOT transcription complex subunit 1 CAF1-binding domain / CCR4-NOT transcription complex subunit 1 TTP binding domain / CCR4-NOT transcription complex subunit 1 HEAT repeat
Similarity search - Domain/homology
: / General negative regulator of transcription subunit 1
Similarity search - Component
Biological speciesSACCHAROMYCES CEREVISIAE S288C (yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.801 Å
AuthorsBasquin, J. / Conti, E.
CitationJournal: Mol.Cell / Year: 2012
Title: Architecture of the Nuclease Module of the Yeast Ccr4-not Complex: The not1-Caf1-Ccr4 Interaction.
Authors: Basquin, J. / Roudko, V.V. / Rode, M. / Basquin, C. / Seraphin, B. / Conti, E.
History
DepositionAug 26, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 21, 2012Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: GENERAL NEGATIVE REGULATOR OF TRANSCRIPTION SUBUNIT 1
B: GENERAL NEGATIVE REGULATOR OF TRANSCRIPTION SUBUNIT 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)142,90931
Polymers137,1972
Non-polymers5,71229
Water0
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6160 Å2
ΔGint-136 kcal/mol
Surface area47130 Å2
MethodPISA
Unit cell
Length a, b, c (Å)55.097, 164.507, 86.141
Angle α, β, γ (deg.)90.00, 100.05, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein GENERAL NEGATIVE REGULATOR OF TRANSCRIPTION SUBUNIT 1 / CELL DIVISION CYCLE PROTEIN 39 / NOT1


Mass: 68598.695 Da / Num. of mol.: 2 / Fragment: N-TERMINAL DOMAIN, RESIDUES 151-753
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE S288C (yeast) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYS STAR / References: UniProt: P25655
#2: Chemical...
ChemComp-AU / GOLD ION


Mass: 196.967 Da / Num. of mol.: 29 / Source method: obtained synthetically / Formula: Au

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.85 Å3/Da / Density % sol: 56.8 % / Description: NONE
Crystal growpH: 7.2 / Details: 2.8 M NACL AND 50 MM TRIS PH 7.2

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.03966
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Apr 21, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03966 Å / Relative weight: 1
ReflectionResolution: 2.8→47.7 Å / Num. obs: 37032 / % possible obs: 99.5 % / Observed criterion σ(I): 2.6 / Redundancy: 4.8 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 20
Reflection shellResolution: 2.8→2.95 Å / Redundancy: 4.8 % / Rmerge(I) obs: 0.53 / Mean I/σ(I) obs: 2.6 / % possible all: 97.1

-
Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
SCALAdata scaling
PHENIXAUTOSOLphasing
RefinementMethod to determine structure: SAD
Starting model: NONE

Resolution: 2.801→46.05 Å / SU ML: 0.44 / σ(F): 1 / Phase error: 33.1 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.2757 1855 5 %
Rwork0.2376 --
obs0.2396 37032 99.72 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 65.276 Å2 / ksol: 0.373 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-21.103 Å20 Å2-19.3617 Å2
2---18.0324 Å20 Å2
3----3.0706 Å2
Refinement stepCycle: LAST / Resolution: 2.801→46.05 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8381 0 29 0 8410
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0098634
X-RAY DIFFRACTIONf_angle_d1.26711696
X-RAY DIFFRACTIONf_dihedral_angle_d16.3033149
X-RAY DIFFRACTIONf_chiral_restr0.0841379
X-RAY DIFFRACTIONf_plane_restr0.0051488
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8007-2.87640.44311410.3722661X-RAY DIFFRACTION97
2.8764-2.9610.41551410.34892685X-RAY DIFFRACTION100
2.961-3.05660.39611440.31922732X-RAY DIFFRACTION100
3.0566-3.16580.35261400.27662647X-RAY DIFFRACTION100
3.1658-3.29250.30041430.26292730X-RAY DIFFRACTION100
3.2925-3.44230.32921450.25742747X-RAY DIFFRACTION100
3.4423-3.62370.25821400.23182653X-RAY DIFFRACTION100
3.6237-3.85070.27791410.23482688X-RAY DIFFRACTION100
3.8507-4.14780.2521440.2132719X-RAY DIFFRACTION100
4.1478-4.56490.2441440.19052732X-RAY DIFFRACTION100
4.5649-5.22460.25581420.20542713X-RAY DIFFRACTION100
5.2246-6.57940.29391440.27152722X-RAY DIFFRACTION100
6.5794-46.05630.21151460.20982748X-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)
10.8894-0.49320.47071.6057-0.04130.91650.0733-0.0726-0.17270.04640.0068-0.04720.20720.0242-0.01970.30580.212-0.1799-0.36690.1682-0.0232-30.1577-0.4975-44.0242
21.1545-1.01811.09995.161-3.4824.90850.0929-0.0423-0.1063-0.44720.14140.3121-0.0871-0.1861-0.24060.5021-0.0761-0.1860.32780.01010.5729-15.9997-44.0144-0.2865
31.10340.61440.49753.7452-1.43973.2509-0.05880.18970.1925-0.06430.0717-0.0917-0.4556-0.13240.07070.2403-0.0474-0.06220.1285-0.04290.31983.6167-37.18931.3276
41.5862-1.09551.18163.7415-2.07453.0146-0.0258-0.2175-0.33230.6440.1367-0.28040.0608-0.1357-0.15140.40230-0.13030.1902-0.00450.4956-19.53426.5808-8.53
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN B AND (RESSEQ 183:464)
2X-RAY DIFFRACTION2CHAIN B AND (RESSEQ 465:746)
3X-RAY DIFFRACTION3CHAIN A AND (RESSEQ 183:463)
4X-RAY DIFFRACTION4CHAIN A AND (RESSEQ 464:746)

+
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