View source for 5tzd


==Structure of the WT S. venezulae BldD-(CTD-c-di-GMP)2 assembly intermediate==
<StructureSection load='5tzd' size='340' side='right'caption='[[5tzd]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5tzd]] is a 4 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=5TZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TZD 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]] 1.749&#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></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=5tzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tzd OCA], [https://pdbe.org/5tzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tzd RCSB], [https://www.ebi.ac.uk/pdbsum/5tzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tzd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F2RCL8_STRVP F2RCL8_STRVP] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Streptomyces are ubiquitous soil bacteria that undergo a complex developmental transition coinciding with their production of antibiotics. This transition is controlled by binding of a novel tetrameric form of the second messenger, 3-5 cyclic diguanylic acid (c-di-GMP) to the master repressor, BldD. In all domains of life, nucleotide-based second messengers allow a rapid integration of external and internal signals into regulatory pathways that control cellular responses to changing conditions. c-di-GMP can assume alternative oligomeric states to effect different functions, binding to effector proteins as monomers, intercalated dimers or, uniquely in the case of BldD, as a tetramer. However, at physiological concentrations c-di-GMP is a monomer and little is known about how higher oligomeric complexes assemble on effector proteins and if intermediates in assembly pathways have regulatory significance. Here, we show that c-di-GMP binds BldD using an ordered, sequential mechanism and that BldD function necessitates the assembly of the BldD2-(c-di-GMP)4 complex.

The Streptomyces master regulator BldD binds c-di-GMP sequentially to create a functional BldD2-(c-di-GMP)4 complex.,Schumacher MA, Zeng W, Findlay KC, Buttner MJ, Brennan RG, Tschowri N Nucleic Acids Res. 2017 Apr 26. doi: 10.1093/nar/gkx287. PMID:28449057<ref>PMID:28449057</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5tzd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces venezuelae ATCC 10712]]
[[Category: Schumacher M]]