1mnm | pdb_00001mnm
YEAST MATALPHA2/MCM1/DNA TERNARY TRANSCRIPTION COMPLEX CRYSTAL STRUCTURE
Structural highlights
Function[MTAL2_YEAST] Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that binds cooperatively with MCM1 to a 31-basepair DNA sequence termed the a-specific gene (asg) operator, to repress the transcription of a-cell-specific genes. Additionally, in a/alpha diploid cells, binds cooperatively with the A1 protein to a 21-basepair DNA sequence termed the haploid-specific gene (hsg) operator, to repress transcription of haploid-specific genes and of MATALPHA1.[1] [MCM1_YEAST] Transcription factor required for the efficient replication of minichromosomes and the transcriptional regulation of early cell cycle genes. Activates transcription of ECB-dependent genes during the G1/M phase. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. Interacts with the alpha-2 repressor or with the alpha-1 activator thereby regulating the expression of mating-type-specific genes. With ARG80, ARG81 and ARG82, coordinates the expression of arginine anabolic and catabolic genes in response to arginine. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe structure of a complex containing the homeodomain repressor protein MATalpha2 and the MADS-box transcription factor MCM1 bound to DNA has been determined by X-ray crystallography at 2.25 A resolution. It reveals the protein-protein interactions responsible for cooperative binding of MATalpha2 and MCM1 to DNA. The otherwise flexible amino-terminal extension of the MATalpha2 homeodomain forms a beta-hairpin that grips the MCM1 surface through parallel beta-strand hydrogen bonds and close-packed, predominantly hydrophobic, side chains. DNA bending induced by MCM1 brings the two proteins closer together, facilitating their interaction. An unusual feature of the complex is that an eight-amino-acid sequence adopts an alpha-helical conformation in one of two copies of the MATalpha2 monomer and a beta-strand conformation in the other. This 'chameleon' sequence of MATalpha2 may be important for recognizing natural operator sites. Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex.,Tan S, Richmond TJ Nature. 1998 Feb 12;391(6668):660-6. PMID:9490409[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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