4ynl

From Proteopedia

(Difference between revisions)

Revision as of 16:13, 2 December 2015

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. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	4yrv
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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] [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.^[2] ^[3] ^[4]

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^[5]

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
↑ Yoon HS, Golden JW. PatS and products of nitrogen fixation control heterocyst pattern. J Bacteriol. 2001 Apr;183(8):2605-13. PMID:11274121 doi:http://dx.doi.org/10.1128/JB.183.8.2605-2613.2001
↑ Huang X, Dong Y, Zhao J. HetR homodimer is a DNA-binding protein required for heterocyst differentiation, and the DNA-binding activity is inhibited by PatS. Proc Natl Acad Sci U S A. 2004 Apr 6;101(14):4848-53. Epub 2004 Mar 29. PMID:15051891 doi:http://dx.doi.org/10.1073/pnas.0400429101
↑ Yoon HS, Golden JW. Heterocyst pattern formation controlled by a diffusible peptide. Science. 1998 Oct 30;282(5390):935-8. PMID:9794762
↑ 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:http://dx.doi.org/10.1038/srep16470

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ynl"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of the hood domain of Anabaena HetR in complex with the hexapeptide ERGSGR derived from PatS==
+<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. 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>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yrv|4yrv]]</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]</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>
+<div style="background-color:#fffaf0;">
+== 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.
-The entry 4ynl is ON HOLD  until Paper Publication
+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<ref>PMID:26576507</ref>
-Authors: Hu, H.X., Jiang, Y.L., Zhao, M.X., Zhang, C.C., Chen, Y., Zhou, C.Z.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of the hood domain of Anabaena HetR in complex with the hexapeptide ERGSGR derived from PatS
+<div class="pdbe-citations 4ynl" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
-[[Category: Zhao, M.X]]
+<references/>
-[[Category: Hu, H.X]]
+__TOC__
+</StructureSection>
 [[Category: Chen, Y]]
-[[Category: Jiang, Y.L]]
+[[Category: Hu, H X]]
-[[Category: Zhang, C.C]]
+[[Category: Jiang, Y L]]
-[[Category: Zhou, C.Z]]
+[[Category: Zhang, C C]]
+[[Category: Zhao, M X]]
+[[Category: Zhou, C Z]]
+[[Category: Heterocyst differentiation]]
+[[Category: Transcription]]
+[[Category: Transcription factor]]

4ynl

From Proteopedia

Revision as of 16:13, 2 December 2015

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

Proteopedia Page Contributors and Editors (what is this?)

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