1mnm: Difference between revisions

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[[Image:1mnm.~~gif~~|left|200px]]

[[Image:1mnm.png|left|200px]]

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~~'''~~YEAST MATALPHA2/MCM1/DNA TERNARY TRANSCRIPTION COMPLEX CRYSTAL STRUCTURE~~'''~~

===YEAST MATALPHA2/MCM1/DNA TERNARY TRANSCRIPTION COMPLEX CRYSTAL STRUCTURE===

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_9490409}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 9490409 is the PubMed ID number.

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==About this Structure==

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[[Category: Transcription regulation]]

[[Category: Transcriptional repression]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ 3 01:27:55 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:29:13 2008''

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-[[Image:1mnm.gif|left|200px]]
+{{Seed}}
+[[Image:1mnm.png|left|200px]]
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 {{STRUCTURE_1mnm|  PDB=1mnm  |  SCENE=  }}
-'''YEAST MATALPHA2/MCM1/DNA TERNARY TRANSCRIPTION COMPLEX CRYSTAL STRUCTURE'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9490409}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9490409 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9490409}}
 ==About this Structure==
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 [[Category: Transcription regulation]]
 [[Category: Transcriptional repression]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 01:27:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul  3 00:29:13 2008''