3qod

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'''Unreleased structure'''
 
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The entry 3qod is ON HOLD
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==Crystal Structure of Heterocyst Differentiation Protein, HetR from Fischerella mv11==
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<StructureSection load='3qod' size='340' side='right'caption='[[3qod]], [[Resolution|resolution]] 3.38&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q2ACK9_9CYAN Q2ACK9_9CYAN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Kim, Y., Joachimiak, G., Gornicki, P., Joachimiak, A., Midwest Center for Structural Genomics (MCSG)
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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>
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Description: Crystal Structure of Heterocyst Differentiation Protein, HetR from Fischerella mv11
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3qod" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Fischerella thermalis PCC 7521]]
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[[Category: Large Structures]]
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[[Category: Gornicki P]]
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[[Category: Joachimiak A]]
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[[Category: Joachimiak G]]
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[[Category: Kim Y]]

Current revision

Crystal Structure of Heterocyst Differentiation Protein, HetR from Fischerella mv11

PDB ID 3qod

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