1le8

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[[Image:1le8.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex==
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|PDB= 1le8 |SIZE=350|CAPTION= <scene name='initialview01'>1le8</scene>, resolution 2.30&Aring;
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<StructureSection load='1le8' size='340' side='right'caption='[[1le8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
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<table><tr><td colspan='2'>[[1le8]] is a 4 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1LE8 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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|GENE= MATalpha2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1le8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1le8 OCA], [https://pdbe.org/1le8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1le8 RCSB], [https://www.ebi.ac.uk/pdbsum/1le8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1le8 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1yrn|1YRN]], [[1akh|1AKH]]
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== Function ==
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|RESOURCES=<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.ebi.ac.uk/pdbsum/1le8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1le8 RCSB]</span>
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[https://www.uniprot.org/uniprot/MATA1_YEASX MATA1_YEASX] Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Transcriptional corepressor that, in a/alpha diploid cells, binds cooperatively with the ALPHA2 protein to a 21-bp DNA sequence termed the haploid-specific gene (hsg) operator, to repress transcription of haploid-specific genes and of MATALPHA1.<ref>PMID:8664541</ref>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''Crystal Structure of the MATa1/MATalpha2-3A Heterodimer Bound to DNA Complex'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/le/1le8_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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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.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1le8 ConSurf].
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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].
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<div style="clear:both"></div>
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== References ==
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==Reference==
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<references/>
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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]
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__TOC__
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[[Category: Protein complex]]
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Ke, A.]]
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[[Category: Ke A]]
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[[Category: Mathias, J R.]]
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[[Category: Mathias JR]]
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[[Category: Vershon, A K.]]
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[[Category: Vershon AK]]
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[[Category: Wolberger, C.]]
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[[Category: Wolberger C]]
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[[Category: isothermal titration calorimetry]]
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[[Category: matalpha2]]
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[[Category: protein-dna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:01:50 2008''
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Current revision

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

PDB ID 1le8

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