4ynl: Difference between revisions

Latest revision as of 15:37, 8 November 2023

Crystal structure of the hood domain of Anabaena HetR in complex with the hexapeptide ERGSGR derived from PatS

Structural highlights

4ynl is a 8 chain structure with sequence from Nostoc sp. PCC 7120 = FACHB-418. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HETR_NOSS1 Controls heterocyst differentiation. Has both a protease and a DNA-binding activity. Binds the promoter regions of hetR, hepA and patS.^[1]

Publication Abstract from PubMed

The one-dimensional pattern of heterocyst in the model cyanobacterium Anabaena sp. PCC 7120 is coordinated by the transcription factor HetR and PatS peptide. Here we report the complex structures of HetR binding to DNA, and its hood domain (HetRHood) binding to a PatS-derived hexapeptide (PatS6) at 2.80 and 2.10 A, respectively. The intertwined HetR dimer possesses a couple of novel HTH motifs, each of which consists of two canonical alpha-helices in the DNA-binding domain and an auxiliary alpha-helix from the flap domain of the neighboring subunit. Two PatS6 peptides bind to the lateral clefts of HetRHood, and trigger significant conformational changes of the flap domain, resulting in dissociation of the auxiliary alpha-helix and eventually release of HetR from the DNA major grove. These findings provide the structural insights into a prokaryotic example of Turing model.

Structural insights into HetR-PatS interaction involved in cyanobacterial pattern formation.,Hu HX, Jiang YL, Zhao MX, Cai K, Liu S, Wen B, Lv P, Zhang Y, Peng J, Zhong H, Yu HM, Ren YM, Zhang Z, Tian C, Wu Q, Oliveberg M, Zhang CC, Chen Y, Zhou CZ Sci Rep. 2015 Nov 18;5:16470. doi: 10.1038/srep16470. PMID:26576507^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Buikema WJ, Haselkorn R. Characterization of a gene controlling heterocyst differentiation in the cyanobacterium Anabaena 7120. Genes Dev. 1991 Feb;5(2):321-30. PMID:1840555
↑ Hu HX, Jiang YL, Zhao MX, Cai K, Liu S, Wen B, Lv P, Zhang Y, Peng J, Zhong H, Yu HM, Ren YM, Zhang Z, Tian C, Wu Q, Oliveberg M, Zhang CC, Chen Y, Zhou CZ. Structural insights into HetR-PatS interaction involved in cyanobacterial pattern formation. Sci Rep. 2015 Nov 18;5:16470. doi: 10.1038/srep16470. PMID:26576507 doi:https://dx.doi.org/10.1038/srep16470

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OCA

[1] Buikema WJ, Haselkorn R. Characterization of a gene controlling heterocyst differentiation in the cyanobacterium Anabaena 7120. Genes Dev. 1991 Feb;5(2):321-30. PMID:1840555

[2] Hu HX, Jiang YL, Zhao MX, Cai K, Liu S, Wen B, Lv P, Zhang Y, Peng J, Zhong H, Yu HM, Ren YM, Zhang Z, Tian C, Wu Q, Oliveberg M, Zhang CC, Chen Y, Zhou CZ. Structural insights into HetR-PatS interaction involved in cyanobacterial pattern formation. Sci Rep. 2015 Nov 18;5:16470. doi: 10.1038/srep16470. PMID:26576507 doi:https://dx.doi.org/10.1038/srep16470

[1]

[2]

@@ Line 3: / Line 3: @@
 <StructureSection load='4ynl' size='340' side='right'caption='[[4ynl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ynl]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_7120 Anabaena 7120]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YNL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YNL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ynl]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YNL FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yrv|4yrv]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hetR, alr2339 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=103690 Anabaena 7120])</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=4ynl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ynl OCA], [https://pdbe.org/4ynl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ynl RCSB], [https://www.ebi.ac.uk/pdbsum/4ynl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ynl ProSAT]</span></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=4ynl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ynl OCA], [http://pdbe.org/4ynl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ynl RCSB], [http://www.ebi.ac.uk/pdbsum/4ynl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ynl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HETR_NOSS1 HETR_NOSS1]] Controls heterocyst differentiation. Has both a protease and a DNA-binding activity. Binds the promoter regions of hetR, hepA and patS.<ref>PMID:1840555</ref>  [[http://www.uniprot.org/uniprot/PATS_NOSS1 PATS_NOSS1]] Inhibits heterocyst differentiation. Seems to control heterocyst pattern formation through intercellular signaling mechanisms. In Anabaena filaments every 10th vegetative cell terminally differentiates into a heterocyst specialized for nitrogen fixation. Seems to inhibit the formation of adjacent heterocysts. Inhibits the DNA-binding of HetR.<ref>PMID:11274121</ref> <ref>PMID:15051891</ref> <ref>PMID:9794762</ref>
+[https://www.uniprot.org/uniprot/HETR_NOSS1 HETR_NOSS1] Controls heterocyst differentiation. Has both a protease and a DNA-binding activity. Binds the promoter regions of hetR, hepA and patS.<ref>PMID:1840555</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Anabaena 7120]]
 [[Category: Large Structures]]
-[[Category: Chen, Y]]
+[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
-[[Category: Hu, H X]]
+[[Category: Chen Y]]
-[[Category: Jiang, Y L]]
+[[Category: Hu HX]]
-[[Category: Zhang, C C]]
+[[Category: Jiang YL]]
-[[Category: Zhao, M X]]
+[[Category: Zhang CC]]
-[[Category: Zhou, C Z]]
+[[Category: Zhao MX]]
-[[Category: Heterocyst differentiation]]
+[[Category: Zhou CZ]]
-[[Category: Transcription]]
-[[Category: Transcription factor]]

4ynl: Difference between revisions

Latest revision as of 15:37, 8 November 2023

Crystal structure of the hood domain of Anabaena HetR in complex with the hexapeptide ERGSGR derived from PatS

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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