View source for 3qod


==Crystal Structure of Heterocyst Differentiation Protein, HetR from Fischerella mv11==
<StructureSection load='3qod' size='340' side='right'caption='[[3qod]], [[Resolution|resolution]] 3.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3qod]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fischerella_thermalis_PCC_7521 Fischerella thermalis PCC 7521]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QOD 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]] 3.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=3qod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qod OCA], [https://pdbe.org/3qod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qod RCSB], [https://www.ebi.ac.uk/pdbsum/3qod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qod ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2ACK9_9CYAN Q2ACK9_9CYAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
HetR is an essential regulator of heterocyst development in cyanobacteria. HetR binds to a DNA palindrome upstream of the hetP gene. We report the crystal structure of HetR from Fischerella at 3.0 A. The protein is a dimer comprised of a central DNA-binding unit containing the N-terminal regions of the two subunits organized with two helix-turn-helix motifs; two globular flaps extending in opposite directions; and a hood over the central core formed from the C-terminal subdomains. The flaps and hood have no structural precedent in the protein database, therefore representing new folds. The structural assignments are supported by site-directed mutagenesis and DNA-binding studies. We suggest that HetR serves as a scaffold for assembly of transcription components critical for heterocyst development.

Structure of transcription factor HetR required for heterocyst differentiation in cyanobacteria.,Kim Y, Joachimiak G, Ye Z, Binkowski TA, Zhang R, Gornicki P, Callahan SM, Hess WR, Haselkorn R, Joachimiak A Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10109-14. Epub 2011 May 31. PMID:21628585<ref>PMID:21628585</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3qod" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Fischerella thermalis PCC 7521]]
[[Category: Large Structures]]
[[Category: Gornicki P]]
[[Category: Joachimiak A]]
[[Category: Joachimiak G]]
[[Category: Kim Y]]