View source for 4oay


==BldD CTD-c-di-GMP complex==
<StructureSection load='4oay' size='340' side='right'caption='[[4oay]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4oay]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_venezuelae_ATCC_10712 Streptomyces venezuelae ATCC 10712]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OAY 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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4oay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oay OCA], [https://pdbe.org/4oay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oay RCSB], [https://www.ebi.ac.uk/pdbsum/4oay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oay ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F2RCL8_STRVP F2RCL8_STRVP] 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4oay" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces venezuelae ATCC 10712]]
[[Category: Brennan RG]]
[[Category: Buttner M]]
[[Category: Schumacher MA]]
[[Category: Tschowri N]]