1LE8

Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex

Summary for 1LE8

• Entry DOI: 10.2210/pdb1le8/pdb
• Related: 1AKH 1YRN
• Descriptor: 5'-D(*AP*CP*AP*TP*GP*TP*AP*AP*AP*AP*AP*TP*TP*TP*AP*CP*AP*TP*CP*A)-3', 5'-D(*TP*TP*GP*AP*TP*GP*TP*AP*AP*AP*TP*TP*TP*TP*TP*AP*CP*AP*TP*G)-3', MATING-TYPE PROTEIN A-1, ... (5 entities in total)
• Functional Keywords: matalpha2, isothermal titration calorimetry, protein-dna complex, transcription-dna complex, transcription/dna
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 4
• Total formula weight: 28167.61

Authors

Ke, A.,Mathias, J.R.,Vershon, A.K.,Wolberger, C. (deposition date: 2002-04-09, release date: 2002-05-03, Last modification date: 2024-02-14)

Primary citation

Ke, A.,Mathias, J.R.,Vershon, A.K.,Wolberger, C.
Structural and Thermodynamic Characterization of the DNA Binding Properties of a Triple Alanine Mutant of MATalpha2
Structure, 10:961-971, 2002

PubMed Abstract: Triply 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.

PubMed: 12121651
DOI: 10.1016/S0969-2126(02)00790-6

Experimental method

X-RAY DIFFRACTION (2.3 Å)