1le8: Difference between revisions
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[[Image:1le8.jpg|left|200px]] | [[Image:1le8.jpg|left|200px]] | ||
'''Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex''' | {{Structure | ||
|PDB= 1le8 |SIZE=350|CAPTION= <scene name='initialview01'>1le8</scene>, resolution 2.30Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= MATalpha2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |||
}} | |||
'''Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LE8 is a [ | 1LE8 is a [[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== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12121651 12121651] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:29:52 2008'' | ||
Revision as of 10:29, 20 March 2008
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| 1le8, resolution 2.30Å | |||||||||||||
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| Gene: | MATalpha2 (Saccharomyces cerevisiae) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex
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.
About this Structure
1LE8 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
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
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