1mnm: Difference between revisions

Revision as of 00:29, 3 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1mnm.png

1mnm, resolution 2.25Å ()

Structural annotation:
Resources:	CATH : 1Mnmc00, 1Mnmd00 InterPro : Ipr002100, Ipr001356, Ipr012287, Ipr009057 Pfam : PF00319, PF00046 SCOP : d1mnma_, d1mnmb_, d1mnmc_, d1mnmd_ UniProt : P11746, Q6B2C0

Functional annotation:
Cellular component:	nuclear chromatin nucleus
Biological process:	regulation of transcription from RNA polymerase II promoter cell cycle transcription DNA replication initiation regulation of transcription, DNA-dependent donor selection regulation of transcription
Molecular function:	DNA bending activity sequence-specific DNA binding transcription factor activity DNA replication origin binding DNA binding

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, RCSB, PDBsum

Coordinates:

save as pdb, mmCIF, xml

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

Template:ABSTRACT PUBMED 9490409

About this StructureAbout this Structure

1MNM is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

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 Thu Jul 3 00:29:13 2008

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OCA

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-'''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.
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+{{ABSTRACT_PUBMED_9490409}}
 ==About this Structure==
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 [[Category: Transcription regulation]]
 [[Category: Transcriptional repression]]
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