5khd: Difference between revisions
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The | ==Structure of 1.75 A BldD C-domain-c-di-GMP complex== | ||
<StructureSection load='5khd' size='340' side='right' caption='[[5khd]], [[Resolution|resolution]] 1.75Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5khd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KHD FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</scene></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=5khd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5khd OCA], [http://pdbe.org/5khd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5khd RCSB], [http://www.ebi.ac.uk/pdbsum/5khd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5khd ProSAT]</span></td></tr> | |||
</table> | |||
<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 5khd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Schumacher, M]] | [[Category: Schumacher, M]] | ||
[[Category: Bldd]] | |||
[[Category: C-di-gmp]] | |||
[[Category: Dna binding protein]] | |||
[[Category: Streptomyce]] | |||
Revision as of 10:29, 13 July 2016
Structure of 1.75 A BldD C-domain-c-di-GMP complex
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