Crystal structure of a yeast TFIIA/TBP/DNA complex

Article Abstract:

A study of the crystal structure of a yeast complex shows that the transcription factor IIA (TFIIA) has a boot-like appearance and consists of a 12-strand beta-barrel and a four-helix bundle motif. The beta-barrel helps in extending the TATA-box-binding protein (TBP) beta-sheet. The beta-barrel assists in bridging over the DNA major groove immediately against the TATA box. The four-helix bundle offers its substantial contribution to the surface of the TFIIA/TBP/DNA complex. The complex interacts with additional transcription factors.

Yeast, Yeast (Food product)

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Structure of serum response factor core bound to DNA

Article Abstract:

A novel protein domain appears responsible for dimerization, DNA binding and collaborating factors' recruitment in the human serum response factor (SRF) core. A three-dimensional structure of this MADS family protein in complex with a particularly identified SRE DNA was determined using X-ray crystallography. This structure may advance the understanding of DNA-binding specificity of all the related SRF and MCM1 accessory proteins especially in the ability to recognize DNA bend sites, allowing it to bind multiple protein factors.

DNA binding proteins

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Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex

Article Abstract:

X-ray crystallography was used to determine the structure of a complex containing the homeodomain repressor protein MATalpha2 and the MADs-box transcription factor MCM1 bound to DNA. Protein-protein interactions leading to cooperative binding of MATalpha2 and MCM1 to DNA are revealed. The amino-terminal extension of the MATalpha2 homeodomain forms a beta-hairpin, gripping the MCM1 surface, and the two proteins are brought closer together, facilitating the interaction.

Usage, Observations, Proteins, X-ray crystallography

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