2CZR

Crystal structure of TBP-interacting protein (Tk-TIP26) and implications for its inhibition mechanism of the interaction between TBP and TATA-DNA

Summary for 2CZR

• Entry DOI: 10.2210/pdb2czr/pdb
• Descriptor: TBP-interacting protein, ZINC ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: tata-binding protein (tbp), tbp-interacting protein (tip), hyperthermophilic archaeon, zn-finger motif, transcription regulator
• Biological source: Thermococcus kodakarensis
• Total number of polymer chains: 1
• Total formula weight: 26155.78

Authors

Yamamoto, T.,Matsuda, T.,Inoue, T.,Matsumura, H.,Morikawa, M.,Kanaya, S.,Kai, Y. (deposition date: 2005-07-15, release date: 2006-02-14, Last modification date: 2024-03-13)

Primary citation

Yamamoto, T.,Matsuda, T.,Inoue, T.,Matsumura, H.,Morikawa, M.,Kanaya, S.,Kai, Y.
Crystal structure of TBP-interacting protein (Tk-TIP26) and implications for its inhibition mechanism of the interaction between TBP and TATA-DNA
Protein Sci., 15:152-161, 2006

PubMed Abstract: TATA-binding protein (TBP)-interacting protein from the hyperthermophilic archaeon Thermococcus kodakaraensis strain KOD1 (Tk-TIP26) is a possible transcription regulatory protein in Thermococcales. Here, we report the crystal structure of Tk-TIP26 determined at 2.3 A resolution with multiple-wavelength anomalous dispersion (MAD) method. The overall structure of Tk-TIP26 consists of two domains. The N-terminal domain forms an alpha/beta structure, in which three alpha-helices enclose the central beta-sheet. The topology of this domain is similar to that of holliday junction resolvase Hjc from Pyrococcus furiosus. The C-terminal domain comprises three alpha-helices, six beta-strands, and two 3(10)-helices. In the dimer structure of Tk-TIP26, two molecules are related with the crystallographic twofold axis, and these molecules rigidly interact with each other via hydrogen bonds. The complex of Tk-TIP26/Tk-TBP is isolated and analyzed by SDS-PAGE and gel filtration column chromatography, resulting in a stoichiometric ratio of the interaction between Tk-TIP26 and Tk-TBP of 4:2, i.e., two dimer molecules of Tk-TIP26 formed a complex with one dimeric TBP. The electrostatic surfaces of Tk-TIP26 and TBP from Pyrocuccus woesei (PwTBP) allowed us to build a model of the Tk-TIP26/TBP complex, and to propose the inhibition mechanism where two dimer molecules of Tk-TIP26 bind to a dimeric TBP, preventing its binding to TATA-DNA.

PubMed: 16322571
DOI: 10.1110/ps.051788906

Experimental method

X-RAY DIFFRACTION (2.3 Å)