6tb4: Difference between revisions
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<StructureSection load='6tb4' size='340' side='right'caption='[[6tb4]], [[Resolution|resolution]] 3.80Å' scene=''> | <StructureSection load='6tb4' size='340' side='right'caption='[[6tb4]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6tb4]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/ ] and [http://en.wikipedia.org/wiki/Komagataella_phaffii_gs115 Komagataella phaffii gs115]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TB4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TB4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6tb4]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824] and [http://en.wikipedia.org/wiki/Komagataella_phaffii_gs115 Komagataella phaffii gs115]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TB4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6TB4 FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6tb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tb4 OCA], [http://pdbe.org/6tb4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tb4 RCSB], [http://www.ebi.ac.uk/pdbsum/6tb4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tb4 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6tb4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tb4 OCA], [http://pdbe.org/6tb4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6tb4 RCSB], [http://www.ebi.ac.uk/pdbsum/6tb4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6tb4 ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/C4QXP2_KOMPG C4QXP2_KOMPG]] Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation), facilitation of DNA opening and initiation of transcription. SAGA is required for recruitment of the basal transcription machinery. SLIK is proposed to have partly overlapping functions with SAGA.[PIRNR:PIRNR017246] | [[http://www.uniprot.org/uniprot/C4QXP2_KOMPG C4QXP2_KOMPG]] Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation), facilitation of DNA opening and initiation of transcription. SAGA is required for recruitment of the basal transcription machinery. SLIK is proposed to have partly overlapping functions with SAGA.[PIRNR:PIRNR017246] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
SAGA (Spt-Ada-Gcn5-acetyltransferase) is a 19-subunit complex that stimulates transcription via two chromatin-modifying enzymatic modules and by delivering the TATA box binding protein (TBP) to nucleate the pre-initiation complex on DNA, a pivotal event in the expression of protein-encoding genes(1). Here we present the structure of yeast SAGA with bound TBP. The core of the complex is resolved at 3.5 A resolution (0.143 Fourier shell correlation). The structure reveals the intricate network of interactions that coordinate the different functional domains of SAGA and resolves an octamer of histone-fold domains at the core of SAGA. This deformed octamer deviates considerably from the symmetrical analogue in the nucleosome and is precisely tuned to establish a peripheral site for TBP, where steric hindrance represses binding of spurious DNA. Complementary biochemical analysis points to a mechanism for TBP delivery and release from SAGA that requires transcription factor IIA and whose efficiency correlates with the affinity of DNA to TBP. We provide the foundations for understanding the specific delivery of TBP to gene promoters and the multiple roles of SAGA in regulating gene expression. | |||
Structure of SAGA and mechanism of TBP deposition on gene promoters.,Papai G, Frechard A, Kolesnikova O, Crucifix C, Schultz P, Ben-Shem A Nature. 2020 Jan;577(7792):711-716. doi: 10.1038/s41586-020-1944-2. Epub 2020 Jan, 22. PMID:31969704<ref>PMID:31969704</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6tb4" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[TATA-binding protein 3D structures|TATA-binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Atcc 18824]] | |||
[[Category: Komagataella phaffii gs115]] | [[Category: Komagataella phaffii gs115]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
Revision as of 10:38, 19 February 2020
Structure of SAGA bound to TBPStructure of SAGA bound to TBP
Structural highlights
Function[C4QXP2_KOMPG] Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation), facilitation of DNA opening and initiation of transcription. SAGA is required for recruitment of the basal transcription machinery. SLIK is proposed to have partly overlapping functions with SAGA.[PIRNR:PIRNR017246] Publication Abstract from PubMedSAGA (Spt-Ada-Gcn5-acetyltransferase) is a 19-subunit complex that stimulates transcription via two chromatin-modifying enzymatic modules and by delivering the TATA box binding protein (TBP) to nucleate the pre-initiation complex on DNA, a pivotal event in the expression of protein-encoding genes(1). Here we present the structure of yeast SAGA with bound TBP. The core of the complex is resolved at 3.5 A resolution (0.143 Fourier shell correlation). The structure reveals the intricate network of interactions that coordinate the different functional domains of SAGA and resolves an octamer of histone-fold domains at the core of SAGA. This deformed octamer deviates considerably from the symmetrical analogue in the nucleosome and is precisely tuned to establish a peripheral site for TBP, where steric hindrance represses binding of spurious DNA. Complementary biochemical analysis points to a mechanism for TBP delivery and release from SAGA that requires transcription factor IIA and whose efficiency correlates with the affinity of DNA to TBP. We provide the foundations for understanding the specific delivery of TBP to gene promoters and the multiple roles of SAGA in regulating gene expression. Structure of SAGA and mechanism of TBP deposition on gene promoters.,Papai G, Frechard A, Kolesnikova O, Crucifix C, Schultz P, Ben-Shem A Nature. 2020 Jan;577(7792):711-716. doi: 10.1038/s41586-020-1944-2. Epub 2020 Jan, 22. PMID:31969704[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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