1le8
From Proteopedia
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| - | [[Image:1le8.jpg|left|200px]] | + | [[Image:1le8.jpg|left|200px]] |
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| - | '''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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| , 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
Page seeded by OCA on Thu Mar 20 12:29:52 2008
