1mh4

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{{STRUCTURE_1mh4| PDB=1mh4 | SCENE= }}
{{STRUCTURE_1mh4| PDB=1mh4 | SCENE= }}
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'''maltose binding-a1 homeodomain protein chimera, crystal form II'''
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===maltose binding-a1 homeodomain protein chimera, crystal form II===
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==Overview==
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The Yeast MATa1 and MATalpha2 are homeodomain proteins that bind DNA cooperatively to repress transcription of cell type specific genes. The DNA affinity and specificity of MATa1 in the absence of MATalpha2, however, is very low. MATa1 is converted to a higher affinity DNA-binding protein by its interaction with the C-terminal tail of MATalpha2. To understand why MATa1 binds DNA weakly by itself, and how the MATalpha2 tail affects the affinity of MATa1 for DNA, we determined the crystal structure of a maltose-binding protein (MBP)-a1 chimera whose DNA binding behavior is similar to MATa1. The overall MATa1 conformation in the MBP-a1 structure, which was determined in the absence of alpha2 and DNA, is similar to that in the a1/alpha2/DNA structure. The sole difference is in the C-terminal portion of the DNA recognition helix of MATa1, which is flexible in the present structure. However, these residues are not in a location likely to be affected by binding of the MATalpha2 tail. The results argue against conformational changes in a1 induced by the tail of MATalpha2, suggesting instead that the MATalpha2 tail energetically couples the DNA binding of MATalpha2 and MATa1.
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(as it appears on PubMed at http://www.pubmed.gov), where 12538894 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12538894}}
==About this Structure==
==About this Structure==
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[[Category: Mata1]]
[[Category: Mata1]]
[[Category: Mbp]]
[[Category: Mbp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:00:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:57:00 2008''

Revision as of 20:57, 2 July 2008

Image:1mh4.png

Template:STRUCTURE 1mh4

maltose binding-a1 homeodomain protein chimera, crystal form II

Template:ABSTRACT PUBMED 12538894

About this Structure

1MH4 is a Single protein structure of sequence from Escherichia coli and saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera., Ke A, Wolberger C, Protein Sci. 2003 Feb;12(2):306-12. PMID:12538894

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