6f3t

Crystal structure of the human TAF5-TAF6-TAF9 complexCrystal structure of the human TAF5-TAF6-TAF9 complex

Structural highlights 6f3t is a 12 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TAF5_HUMAN TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription. TAF5/TAFII100 interacts strongly with the histone H4-related TAF6/TAFII80 and the histone H3-related TAF9/TAFII31, as well as a stable complex comprised of both TAF5/TAFII80 and TAF6/TAFII31. Apparently weaker interactions of TAF5/TAFII100 with TBP, TAF1/TAFII250, TAF11/TAFII28, and TAF12/TAFII20, but not TAF7/TAFII55, also have been observed. Publication Abstract from PubMed TFIID is a cornerstone of eukaryotic gene regulation. Distinct TFIID complexes with unique subunit compositions exist and several TFIID subunits are shared with other complexes, thereby conveying precise cellular control of subunit allocation and functional assembly of this essential transcription factor. However, the molecular mechanisms that underlie the regulation of TFIID remain poorly understood. Here we use quantitative proteomics to examine TFIID submodules and assembly mechanisms in human cells. Structural and mutational analysis of the cytoplasmic TAF5-TAF6-TAF9 submodule identified novel interactions that are crucial for TFIID integrity and for allocation of TAF9 to TFIID or the Spt-Ada-Gcn5 acetyltransferase (SAGA) co-activator complex. We discover a key checkpoint function for the chaperonin CCT, which specifically associates with nascent TAF5 for subsequent handover to TAF6-TAF9 and ultimate holo-TFIID formation. Our findings illustrate at the molecular level how multisubunit complexes are generated within the cell via mechanisms that involve checkpoint decisions facilitated by a chaperone. Chaperonin CCT checkpoint function in basal transcription factor TFIID assembly.,Antonova SV, Haffke M, Corradini E, Mikuciunas M, Low TY, Signor L, van Es RM, Gupta K, Scheer E, Vos HR, Tora L, Heck AJR, Timmers HTM, Berger I Nat Struct Mol Biol. 2018 Dec;25(12):1119-1127. doi: 10.1038/s41594-018-0156-z., Epub 2018 Dec 3. PMID:30510221 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transcription initiation factors 3D structures

spinqualitylabelsall models 6f3t, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image