PDBsum entry: 1ais

Transcription/DNA

PDB-id: 1ais

Biological unit* = asymmetric unit, as shown
(*as deduced by PQS)

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PROCHECK

Protein chains

181 a.a. *

193 a.a. *

DNA/RNA

Waters ×288

* Residue conservation analysis

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PDB id:

1ais

Name:

Transcription/DNA

Title:

Tata-binding protein/transcription factor (ii)b/tata-box complex from pyrococcus woesei

Structure:

DNA (5'-d( Ap Ap Cp Tp Tp Ap Cp Tp Tp Tp (5Iu) p (5Iu)p Ap Ap Ap Gp C)-3'). Chain: c. Engineered: yes. DNA (5'- d( Gp Cp Tp Tp Tp Ap Ap Ap Ap Ap Gp Tp Ap Ap Gp Tp T )-3'). Chain: e. Engineered: yes. Protein (tata-binding protein).

Source:

Synthetic: yes. Pyrococcus woesei. Organism_taxid: 2262. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: de3.

Biological unit:

Tetramer (from PQS)

UniProt:

Chain A: P62001 (TBP_PYRWO)

Seq:	191 a.a.
Struc:	181 a.a.

Chain B: P61999 (TF2B_PYRWO)

Seq:

Struc:

Seq:

300 a.a.

Struc:

193 a.a.

Key:	PfamA domain
Secondary structure	CATH domain

Resolution:

2.10Å

R-factor:

0.212

R-free:

0.268

Authors:

P.F.Kosa,G.Ghosh,B.S.Dedecker,P.B.Sigler

Key ref:

P.F.Kosa et al. (1997). The 2.1-A crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-box.. Proc Natl Acad Sci U S A, 94, 6042-6047. [PubMed id: 9177165] [DOI: 10.1073/pnas.94.12.6042]

Date:

24-Apr-97

Release date:

07-Jul-97

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Key reference

DOI no: 10.1073/pnas.94.12.6042

Proc Natl Acad Sci U S A 94:6042-6047 (1997)

PubMed id: 9177165

The 2.1-A crystal structure of an archaeal preinitiation complex: TATA-box-binding protein/transcription factor (II)B core/TATA-box.

P.F.Kosa, G.Ghosh, B.S.DeDecker, P.B.Sigler.

ABSTRACT

Archaea possess a basal transcriptional apparatus that resembles that of eukaryotes. Here we report the 2.1-A crystal structure of the archaeal transcription factor complex formed by the TATA-box-binding protein (TBP), the transcription factor IIB homolog, and a DNA target, all from the hyperthermophile Pyrococcus woesei. The overall fold of these two basal transcription factors is essentially the same as that of their eukaryotic counterparts. However, in comparison with the eukaryotic complexes, the archaeal TBP-DNA interface is more symmetrical, and in this structure the orientation of the preinitiation complex assembly on the promoter is inverted with respect to that seen in all crystal structures of comparable eukaryotic systems. This study of the structural details of an archaeal transcription factor complex presents the opportunity to examine the evolution of the basal eukaryotic transcriptional apparatus from a stereochemical viewpoint and to extend our understanding of the physical biochemistry of transcriptional initiation.

Selected figure(s)

Figure 2.
Fig. 2. Stereo pair of electron density of a sigma A weighted (26) 2|F[o]| |F[c]| map, contoured at 2 . pwTFB[c] residues are magenta, pwTBP residues are white, DNA is yellow, and water molecules are^ orange spheres.

Figure 3.
Fig. 3. (a) Ribbons (28) drawing of the overall structure of the ternary complex. pwTBP is in red, the N-terminal domain of pwTFB[c]^ is green, the C-terminal domain is yellow, and DNA is blue. (b) Stereo drawing of pwTFB[c], with the same orientation as in a.

Figures were selected by the author.