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 2.250&Aring;" /> '''YEAST MATALPHA2/MCM...)
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[[Image:1mnm.gif|left|200px]]<br /><applet load="1mnm" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mnm, resolution 2.250&Aring;" />
caption="1mnm, resolution 2.250&Aring;" />
'''YEAST MATALPHA2/MCM1/DNA TERNARY TRANSCRIPTION COMPLEX CRYSTAL STRUCTURE'''<br />
'''YEAST MATALPHA2/MCM1/DNA TERNARY TRANSCRIPTION COMPLEX CRYSTAL STRUCTURE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1MNM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MNM OCA].
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1MNM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MNM OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Tan, T.J.Richmond S.]]
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[[Category: Tan, T J.Richmond S.]]
[[Category: complex (transcription/homeobox/dna)]]
[[Category: complex (transcription/homeobox/dna)]]
[[Category: dna-binding protein]]
[[Category: dna-binding protein]]
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[[Category: transcriptional repression]]
[[Category: transcriptional repression]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:33:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:08 2008''

Revision as of 11:57, 21 February 2008

Image:1mnm.gif

1mnm, resolution 2.250Å

Drag the structure with the mouse to rotate

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

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