United States, European Union, Switzerland, 6 items
Organization
Grant number
Country
Howard Hughes Medical Institute (HHMI)
CC30250
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R35GM127018
United States
European Molecular Biology Organization (EMBO)
ALTF 1002-2018
European Union
Swiss National Science Foundation
P2BSP3_181878
Switzerland
Howard Hughes Medical Institute (HHMI)
CC34430
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
T32GM098218
United States
Citation
Journal: Nat Struct Mol Biol / Year: 2021 Title: Structure of the human SAGA coactivator complex. Authors: Dominik A Herbst / Meagan N Esbin / Robert K Louder / Claire Dugast-Darzacq / Gina M Dailey / Qianglin Fang / Xavier Darzacq / Robert Tjian / Eva Nogales / Abstract: The SAGA complex is a regulatory hub involved in gene regulation, chromatin modification, DNA damage repair and signaling. While structures of yeast SAGA (ySAGA) have been reported, there are ...The SAGA complex is a regulatory hub involved in gene regulation, chromatin modification, DNA damage repair and signaling. While structures of yeast SAGA (ySAGA) have been reported, there are noteworthy functional and compositional differences for this complex in metazoans. Here we present the cryogenic-electron microscopy (cryo-EM) structure of human SAGA (hSAGA) and show how the arrangement of distinct structural elements results in a globally divergent organization from that of yeast, with a different interface tethering the core module to the TRRAP subunit, resulting in a dramatically altered geometry of functional elements and with the integration of a metazoan-specific splicing module. Our hSAGA structure reveals the presence of an inositol hexakisphosphate (InsP) binding site in TRRAP and an unusual property of its pseudo-(Ψ)PIKK. Finally, we map human disease mutations, thus providing the needed framework for structure-guided drug design of this important therapeutic target for human developmental diseases and cancer.
History
Deposition
Nov 24, 2020
-
Header (metadata) release
Nov 10, 2021
-
Map release
Nov 10, 2021
-
Update
May 29, 2024
-
Current status
May 29, 2024
Processing site: RCSB / Status: Released
-
Structure visualization
Movie
Surface view with section colored by density value
Protein or peptide: Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein,Transformation/transcription domain-associated protein
Protein or peptide: TAF5-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 5L
Protein or peptide: Isoform 3 of Transcription factor SPT20 homolog
Protein or peptide: Transcription initiation factor TFIID subunit 9B
Protein or peptide: TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L,TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L,TAF6-like RNA polymerase II p300/CBP-associated factor-associated factor 65 kDa subunit 6L
Protein or peptide: Transcription initiation factor TFIID subunit 12
Protein or peptide: Transcription initiation factor TFIID subunit 10
Protein or peptide: Transcription initiation protein SPT3 homolog,Transcription initiation protein SPT3 homolog,Transcription initiation protein SPT3 homolog
In the structure databanks used in Yorodumi, some data are registered as the other names, "COVID-19 virus" and "2019-nCoV". Here are the details of the virus and the list of structure data.
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
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