3qod: Difference between revisions
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==Crystal Structure of Heterocyst Differentiation Protein, HetR from Fischerella mv11== | |||
<StructureSection load='3qod' size='340' side='right' caption='[[3qod]], [[Resolution|resolution]] 3.38Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3qod]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fischerella_thermalis Fischerella thermalis]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QOD FirstGlance]. <br> | |||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qoe|3qoe]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hetR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=372787 Fischerella thermalis])</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=3qod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qod RCSB], [http://www.ebi.ac.uk/pdbsum/3qod PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Fischerella thermalis]] | [[Category: Fischerella thermalis]] | ||
[[Category: Gornicki, P | [[Category: Gornicki, P]] | ||
[[Category: Joachimiak, A | [[Category: Joachimiak, A]] | ||
[[Category: Joachimiak, G | [[Category: Joachimiak, G]] | ||
[[Category: Kim, Y | [[Category: Kim, Y]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Cytosol]] | [[Category: Cytosol]] | ||
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Helix-turn-helix]] | [[Category: Helix-turn-helix]] | ||
[[Category: Mcsg]] | [[Category: Mcsg]] | ||
[[Category: Psi-biology]] | [[Category: Psi-biology]] | ||
[[Category: Transcription factor]] | [[Category: Transcription factor]] | ||
