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Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA ComplexCrystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex
Structural highlights
Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTriply mutated MATalpha2 protein, alpha2-3A, in which all three major groove-contacting residues are mutated to alanine, is defective in binding DNA alone or in complex with Mcm1 yet binds with MATa1 with near wild-type affinity and specificity. To gain insight into this unexpected behavior, we determined the crystal structure of the a1/alpha2-3A/DNA complex. The structure shows that the triple mutation causes a collapse of the alpha2-3A/DNA interface that results in a reorganized set of alpha2-3A/DNA contacts, thereby enabling the mutant protein to recognize the wild-type DNA sequence. Isothermal titration calorimetry measurements reveal that a much more favorable entropic component stabilizes the a1/alpha2-3A/DNA complex than the alpha2-3A/DNA complex. The combined structural and thermodynamic studies provide an explanation of how partner proteins influence the sequence specificity of a DNA binding protein. Structural and thermodynamic characterization of the DNA binding properties of a triple alanine mutant of MATalpha2.,Ke A, Mathias JR, Vershon AK, Wolberger C Structure. 2002 Jul;10(7):961-71. PMID:12121651[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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