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PDBsum entry 2nxp
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Transcription
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PDB id
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2nxp
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References listed in PDB file
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Key reference
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Title
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Structural analysis and dimerization potential of the human taf5 subunit of tfiid.
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Authors
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S.Bhattacharya,
S.Takada,
R.H.Jacobson.
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Ref.
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Proc Natl Acad Sci U S A, 2007,
104,
1189-1194.
[DOI no: ]
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PubMed id
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Abstract
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TFIID is an essential factor required for RNA polymerase II transcription but
remains poorly understood because of its intrinsic complexity. Human TAF5, a
100-kDa subunit of general transcription factor TFIID, is an essential gene and
plays a critical role in assembling the 1.2 MDa TFIID complex. We report here a
structural analysis of the TAF5 protein. Our structure at 2.2-A resolution of
the TAF5-NTD2 domain reveals an alpha-helical domain with distant structural
similarity to RNA polymerase II CTD interacting factors. The TAF5-NTD2 domain
contains several conserved clefts likely to be critical for TFIID complex
assembly. Our biochemical analysis of the human TAF5 protein demonstrates the
ability of the N-terminal half of the TAF5 gene to form a flexible, extended
dimer, a key property required for the assembly of the TFIID complex.
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Figure 1.
Fig. 1. Primary sequence organization of hTAF5. Schematic
diagram of the domain structure present in human TAF5 where
NTD1/LisH corresponds to LIS1 homology domain (29), NTD2
corresponds to the  -helical domain
reported here, and WD40 repeats are predicted to form a closed
 -propeller structure.
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Figure 2.
Fig. 2. Structure of the hTAF5-NTD2 domain. (a) Diagram of
the hTAF5-NTD2. (b) Top view of the -helical domain of the
hTAF5-NTD2 showing the arrangement of the other helices around
the central helix ( 3) in the crystal
structure. All of the helices and the strands are labeled. Two
views in a and b are related by rotation of 90° around a
horizontal axis. (c) Topology diagram of the secondary
structural elements of the hTAF5-NTD2 domain to show the
arrangement of the helical bundle (front view) and the helical
sheet (back view) of the crystal structure.
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