View source for 6alx


==Structure of F. tularensis MglA-SspA solved in the presence of polyP==
<StructureSection load='6alx' size='340' side='right'caption='[[6alx]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6alx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis Francisella tularensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ALX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ALX 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]] 3.3&#8491;</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=6alx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6alx OCA], [https://pdbe.org/6alx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6alx RCSB], [https://www.ebi.ac.uk/pdbsum/6alx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6alx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0E2ZLH6_FRATU A0A0E2ZLH6_FRATU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Francisella tularensis, the etiological agent of tularemia, is one of the most infectious bacteria known. Because of its extreme pathogenicity, F. tularensis is classified as a category A bioweapon by the US government. F. tularensis virulence stems from genes encoded on the Francisella pathogenicity island (FPI). An unusual set of Francisella regulators-the heteromeric macrophage growth locus protein A (MglA)-stringent starvation protein A (SspA) complex and the DNA-binding protein pathogenicity island gene regulator (PigR)-activates FPI transcription and thus is essential for virulence. Intriguingly, the second messenger, guanosine-tetraphosphate (ppGpp), which is produced during infection, is also involved in coordinating Francisella virulence; however, its role has been unclear. Here we identify MglA-SspA as a novel ppGpp-binding complex and describe structures of apo- and ppGpp-bound MglA-SspA. We demonstrate that MglA-SspA, which binds RNA polymerase (RNAP), also interacts with the C-terminal domain of PigR, thus anchoring the (MglA-SspA)-RNAP complex to the FPI promoter. Furthermore, we show that MglA-SspA must be bound to ppGpp to mediate high-affinity interactions with PigR. Thus, these studies unveil a novel pathway different from those described previously for regulation of transcription by ppGpp. The data also indicate that F. tularensis pathogenesis is controlled by a highly interconnected molecular circuitry in which the virulence machinery directly senses infection via a small molecule stress signal.

Dissection of the molecular circuitry controlling virulence in Francisella tularensis.,Cuthbert BJ, Ross W, Rohlfing AE, Dove SL, Gourse RL, Brennan RG, Schumacher MA Genes Dev. 2017 Aug 1;31(15):1549-1560. doi: 10.1101/gad.303701.117. Epub 2017, Sep 1. PMID:28864445<ref>PMID:28864445</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6alx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Stringent starvation protein 3D structures|Stringent starvation protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Francisella tularensis]]
[[Category: Large Structures]]
[[Category: Schumacher MA]]