ArticleProtein science : a publication of the Protein Society2003
Insights into binding cooperativity of MATa1/MATalpha2 from the crystal structure of a MATa1 homeodomain-maltose binding protein chimera.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 45 citations in OpenAlex.
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- The "Sticky Patch" Model of Crystallization and Modification of Proteins for Enhanced Crystallizability.Methods in molecular biology (Clifton, N.J.) · 2017Review
- Crystal structures of MBP fusion proteins.Protein science : a publication of the Protein Society · 2016Review
- Protein stability: a crystallographer's perspective.Acta crystallographica. Section F, Structural biology communications · 2016Review
- Fusion-protein-assisted protein crystallization.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Mechanistic strategies for catalysis adopted by evolutionary distinct family 43 arabinanases.The Journal of biological chemistry · 2014Article
- To fuse or not to fuse: what is your purpose?Protein science : a publication of the Protein Society · 2013Review
- Improved expression and purification of sigma 1 receptor fused to maltose binding protein by alteration of linker sequence.Protein expression and purification · 2013Article
- SIMS: a hybrid method for rapid conformational analysis.PloS one · 2013Article
- Cooperative DNA-binding and sequence-recognition mechanism of aristaless and clawless.The EMBO journal · 2010Article
- Application of protein engineering to enhance crystallizability and improve crystal properties.Acta crystallographica. Section D, Biological crystallography · 2010Article
- A synergistic approach to protein crystallization: combination of a fixed-arm carrier with surface entropy reduction.Protein science : a publication of the Protein Society · 2010Review
- Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process.Protein science : a publication of the Protein Society · 2009Article
- Thioredoxin as a fusion tag for carrier-driven crystallization.Protein science : a publication of the Protein Society · 2008Article
- Cloning, expression, purification and preliminary crystallographic analysis of the RNase HI domain of the Mycobacterium tuberculosis protein Rv2228c as a maltose-binding protein fusion.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
- Crystal structure of human IPS-1/MAVS/VISA/Cardif caspase activation recruitment domain.BMC structural biology · 2008Article
- A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production.BMC biotechnology · 2006Article
- Arm-domain interactions can provide high binding cooperativity.Protein science : a publication of the Protein Society · 2004Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
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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