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| <StructureSection load='4m8b' size='340' side='right'caption='[[4m8b]], [[Resolution|resolution]] 2.61Å' scene=''> | | <StructureSection load='4m8b' size='340' side='right'caption='[[4m8b]], [[Resolution|resolution]] 2.61Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[4m8b]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M8B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M8B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4m8b]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M8B FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YHR177W, Yhr177wp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4m8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m8b OCA], [https://pdbe.org/4m8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m8b RCSB], [https://www.ebi.ac.uk/pdbsum/4m8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m8b ProSAT]</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=4m8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m8b OCA], [http://pdbe.org/4m8b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m8b RCSB], [http://www.ebi.ac.uk/pdbsum/4m8b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m8b ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/YHX7_YEAST YHX7_YEAST] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Baker's yeast]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Johnson, A D]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
- | [[Category: Lohse, M L]] | + | [[Category: Johnson AD]] |
- | [[Category: Rosenberg, O S]] | + | [[Category: Lohse ML]] |
- | [[Category: Stroud, R M]] | + | [[Category: Rosenberg OS]] |
- | [[Category: Transcription]] | + | [[Category: Stroud RM]] |
- | [[Category: Transcription factor]]
| + | |
- | [[Category: Transcription-dna complex]]
| + | |
- | [[Category: Wopr domain]]
| + | |
- | [[Category: Wopr fungal-pathogenesis transcription]]
| + | |
| Structural highlights
Function
YHX7_YEAST
Publication Abstract from PubMed
WOPR-domain proteins are found throughout the fungal kingdom where they function as master regulators of cell morphology and pathogenesis. Genetic and biochemical experiments previously demonstrated that these proteins bind to specific DNA sequences and thereby regulate transcription. However, their primary sequence showed no relationship to any known DNA-binding domain, and the basis for their ability to recognize DNA sequences remained unknown. Here, we describe the 2.6-A crystal structure of a WOPR domain in complex with its preferred DNA sequence. The structure reveals that two highly conserved regions, separated by an unconserved linker, form an interdigitated beta-sheet that is tilted into the major groove of DNA. Although the main interaction surface is in the major groove, the highest-affinity interactions occur in the minor groove, primarily through a deeply penetrating arginine residue. The structure reveals a new, unanticipated mechanism by which proteins can recognize specific sequences of DNA.
Structure of a new DNA-binding domain which regulates pathogenesis in a wide variety of fungi.,Lohse MB, Rosenberg OS, Cox JS, Stroud RM, Finer-Moore JS, Johnson AD Proc Natl Acad Sci U S A. 2014 Jul 3. pii: 201410110. PMID:24994900[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lohse MB, Rosenberg OS, Cox JS, Stroud RM, Finer-Moore JS, Johnson AD. Structure of a new DNA-binding domain which regulates pathogenesis in a wide variety of fungi. Proc Natl Acad Sci U S A. 2014 Jul 3. pii: 201410110. PMID:24994900 doi:http://dx.doi.org/10.1073/pnas.1410110111
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