1le8: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1le8]] is a 4 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LE8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1le8]] is a 4 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LE8 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yrn|1yrn]], [[1akh|1akh]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yrn|1yrn]], [[1akh|1akh]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MATalpha2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MATalpha2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1le8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1le8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1le8 RCSB], [http://www.ebi.ac.uk/pdbsum/1le8 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1le8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1le8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1le8 RCSB], [http://www.ebi.ac.uk/pdbsum/1le8 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Ke, A | [[Category: Ke, A]] | ||
[[Category: Mathias, J R | [[Category: Mathias, J R]] | ||
[[Category: Vershon, A K | [[Category: Vershon, A K]] | ||
[[Category: Wolberger, C | [[Category: Wolberger, C]] | ||
[[Category: Isothermal titration calorimetry]] | [[Category: Isothermal titration calorimetry]] | ||
[[Category: Matalpha2]] | [[Category: Matalpha2]] | ||
[[Category: Protein-dna complex]] | [[Category: Protein-dna complex]] | ||
[[Category: Transcription-dna complex]] | [[Category: Transcription-dna complex]] | ||
Revision as of 19:25, 5 January 2015
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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