1le8: Difference between revisions

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[[Image:1le8.jpg|left|200px]]<br /><applet load="1le8" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1le8.jpg|left|200px]]<br /><applet load="1le8" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1le8, resolution 2.30Å" />

'''Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex'''<br />

==Overview==

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.

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.

==About this Structure==

1LE8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1LE8 OCA].

1LE8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE8 OCA].

==Reference==

Line 14:

[[Category: Saccharomyces cerevisiae]]

[[Category: Ke, A.]]

[[Category: Mathias, J.R.]]

[[Category: Mathias, J R.]]

[[Category: Vershon, A.K.]]

[[Category: Vershon, A K.]]

[[Category: Wolberger, C.]]

[[Category: isothermal titration calorimetry]]

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[[Category: protein-dna complex]]

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@@ Line 1: / Line 1: @@
-[[Image:1le8.jpg|left|200px]]<br /><applet load="1le8" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1le8.jpg|left|200px]]<br /><applet load="1le8" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1le8, resolution 2.30&Aring;" />
 '''Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-LE8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LE8 OCA].
+LE8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE8 OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Ke, A.]]
-[[Category: Mathias, J.R.]]
+[[Category: Mathias, J R.]]
-[[Category: Vershon, A.K.]]
+[[Category: Vershon, A K.]]
 [[Category: Wolberger, C.]]
 [[Category: isothermal titration calorimetry]]
@@ Line 21: / Line 21: @@
 [[Category: protein-dna complex]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:30:33 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:14 2008''