[English] 日本語
Yorodumi
- SASDA56: BAZ2B in Tris (Bromodomain adjacent to zinc finger domain protein... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: SASBDB / ID: SASDA56
SampleBAZ2B in Tris
  • Bromodomain adjacent to zinc finger domain protein 2B, C-terminal (protein), BAZ2B, Homo sapiens
Biological speciesHomo sapiens (human)
CitationJournal: Structure / Year: 2015
Title: Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC.
Authors: Cynthia Tallant / Erica Valentini / Oleg Fedorov / Lois Overvoorde / Fleur M Ferguson / Panagis Filippakopoulos / Dmitri I Svergun / Stefan Knapp / Alessio Ciulli /
Abstract: Binding of the chromatin remodeling complex NoRC to RNA complementary to the rDNA promoter mediates transcriptional repression. TIP5, the largest subunit of NoRC, is involved in recruitment to rDNA ...Binding of the chromatin remodeling complex NoRC to RNA complementary to the rDNA promoter mediates transcriptional repression. TIP5, the largest subunit of NoRC, is involved in recruitment to rDNA by interactions with promoter-bound TTF-I, pRNA, and acetylation of H4K16. TIP5 domains that recognize posttranslational modifications on histones are essential for recruitment of NoRC to chromatin, but how these reader modules recognize site-specific histone tails has remained elusive. Here, we report crystal structures of PHD zinc finger and bromodomains from human TIP5 and BAZ2B in free form and bound to H3 and/or H4 histones. PHD finger functions as an independent structural module in recognizing unmodified H3 histone tails, and the bromodomain prefers H3 and H4 acetylation marks followed by a key basic residue, KacXXR. Further low-resolution analyses of PHD-bromodomain modules provide molecular insights into their trans histone tail recognition, required for nucleosome recruitment and transcriptional repression of the NoRC complex.
Contact author
  • Erica Valentini (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Models

Model #159
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196
Search similar-shape structures of this assembly by Omokage search (details)
Model #160
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196
Search similar-shape structures of this assembly by Omokage search (details)
Model #161
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196
Search similar-shape structures of this assembly by Omokage search (details)
Model #162
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196
Search similar-shape structures of this assembly by Omokage search (details)
Model #163
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196
Search similar-shape structures of this assembly by Omokage search (details)
Model #164
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196
Search similar-shape structures of this assembly by Omokage search (details)
Model #165
Type: mix / Software: EOM / Radius of dummy atoms: 1.90 A / Chi-square value: 1.028196
Search similar-shape structures of this assembly by Omokage search (details)

-
Sample

SampleName: BAZ2B in Tris / Specimen concentration: 10 mg/ml
BufferName: Tris / Concentration: 20.00 mM / pH: 8
Composition: NaCl 500.000 mM, DTT 2.000 mM, ZnCl2 10.000 microM
Entity #115Name: BAZ2B / Type: protein
Description: Bromodomain adjacent to zinc finger domain protein 2B, C-terminal
Formula weight: 27.67 / Num. of mol.: 1 / Source: Homo sapiens
Sequence: AMASIMKVYC QICRKGDNEE LLLLCDGCDK GCHTYCHRPK ITTIPDGDWF CPACIAKASG QTLKIKKLHV KGKKTNESKK GKKVTLTGDT EDEDSASTSS SLKRGNKDLK KRKMEENTSI NLSKQESFTS VKKPKRDDSK DLALCSMILT EMETHEDAWP FLLPVNLKLV ...Sequence:
AMASIMKVYC QICRKGDNEE LLLLCDGCDK GCHTYCHRPK ITTIPDGDWF CPACIAKASG QTLKIKKLHV KGKKTNESKK GKKVTLTGDT EDEDSASTSS SLKRGNKDLK KRKMEENTSI NLSKQESFTS VKKPKRDDSK DLALCSMILT EMETHEDAWP FLLPVNLKLV PGYKKVIKKP MDFSTIREKL SSGQYPNLET FALDVRLVFD NCETFNEDDS DIGRAGHNMR KYFEKKWTDT FKVS

-
Experimental information

BeamInstrument name: DORIS III X33 / City: Hamburg / : Germany / Shape: 0.6 / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.15 Å / Dist. spec. to detc.: 2.7 mm
DetectorName: Pilatus 1M-W / Pixsize x: 0.172 mm
Scan
Title: BAZ2B in Tris / Measurement date: Sep 24, 2012 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 15 sec. / Number of frames: 8 / Unit: 1/nm /
MinMax
Q0.0871 6.0145
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 434 /
MinMax
Q0.09259 6.012
P(R) point1 434
R0 15
Result
Type of curve: single_conc /
ExperimentalStandardPorod
MW25 kDa33 kDa25 kDa
Volume--43 nm3

P(R)Guinier
Forward scattering, I028.5 28
Radius of gyration, Rg4.2 nm4 nm

MinMax
D-14.5
Guinier point30 91

+
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