1mnm
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(New page: 200px<br /><applet load="1mnm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mnm, resolution 2.250Å" /> '''YEAST MATALPHA2/MCM...)
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Revision as of 19:26, 20 November 2007
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YEAST MATALPHA2/MCM1/DNA TERNARY TRANSCRIPTION COMPLEX CRYSTAL STRUCTURE
Overview
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. 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.
About this Structure
1MNM is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the yeast MATalpha2/MCM1/DNA ternary complex., Tan S, Richmond TJ, Nature. 1998 Feb 12;391(6668):660-6. PMID:9490409
Page seeded by OCA on Tue Nov 20 21:33:36 2007
