The 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.
MtrF is a cell surface cytochrome on the Gram-negative bacteria known as Shewanella oneidensis.[1] MtrF is involved with shuttling electrons across its (S. oneidensis) outer surface. MtrF has several homologues, MtrC and the protein OmcA. These three different proteins are thought to be replaceable with one another in deletion mutation experiments.[1]
Secuencia desde N a C terminal
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Structure
Through the structure of this oligomer that was obtained by crystallography, we can see that HDAC9 is kept relatively far from the genomic DNA even after MEF2 binding to the chromosome. We can also easily observe a very well evolutionary conserved region near the DNA binding site of MEF2.
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- ↑ 1.0 1.1 Fotinou C, Emsley P, Black I, Ando H, Ishida H, Kiso M, Sinha KA, Fairweather NF, Isaacs NW. The crystal structure of tetanus toxin Hc fragment complexed with a synthetic GT1b analogue suggests cross-linking between ganglioside receptors and the toxin. J Biol Chem. 2001 Aug 24;276(34):32274-81. Epub 2001 Jun 19. PMID:11418600 doi:10.1074/jbc.M103285200
