4ob4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the S. venezulae BldD DNA-binding domain== | |
| + | <StructureSection load='4ob4' size='340' side='right'caption='[[4ob4]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ob4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OB4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OB4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=4ob4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ob4 OCA], [https://pdbe.org/4ob4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ob4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ob4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ob4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q7AKQ8_STRCO Q7AKQ8_STRCO] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The cyclic dinucleotide c-di-GMP is a signaling molecule with diverse functions in cellular physiology. Here, we report that c-di-GMP can assemble into a tetramer that mediates the effective dimerization of a transcription factor, BldD, which controls the progression of multicellular differentiation in sporulating actinomycete bacteria. BldD represses expression of sporulation genes during vegetative growth in a manner that depends on c-di-GMP-mediated dimerization. Structural and biochemical analyses show that tetrameric c-di-GMP links two subunits of BldD through their C-terminal domains, which are otherwise separated by ~10 A and thus cannot effect dimerization directly. Binding of the c-di-GMP tetramer by BldD is selective and requires a bipartite RXD-X8-RXXD signature. The findings indicate a unique mechanism of protein dimerization and the ability of nucleotide signaling molecules to assume alternative oligomeric states to effect different functions. | ||
| - | + | Tetrameric c-di-GMP mediates effective transcription factor dimerization to control Streptomyces development.,Tschowri N, Schumacher MA, Schlimpert S, Chinnam NB, Findlay KC, Brennan RG, Buttner MJ Cell. 2014 Aug 28;158(5):1136-47. doi: 10.1016/j.cell.2014.07.022. PMID:25171413<ref>PMID:25171413</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4ob4" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Brennan R]] | ||
| + | [[Category: Buttner M]] | ||
| + | [[Category: Tschowri N]] | ||
| + | [[Category: Schumacher MA]] | ||
Current revision
Structure of the S. venezulae BldD DNA-binding domain
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