8pb9

From Proteopedia

(Difference between revisions)

Revision as of 11:45, 13 December 2023

Cryo-EM structure of the c-di-GMP-bound FleQ-FleN master regulator complex from Pseudomonas aeruginosa

Structural highlights

8pb9 is a 5 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.3Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FLEQ_PSEAE AAA+ ATPase enhancer-binding protein that acts as a transcription regulator and plays a role in the modulation of mucin adhesion and flagellar gene expression (PubMed:9287015, PubMed:11673434, PubMed:26362077). In addition to flagella genes, regulates also expression of biofilm-related genes (PubMed:22581773). Functions as a transcriptional repressor in the absence of c-di-GMP and as an activator when c-di-GMP is present (PubMed:22581773).^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Pseudomonas aeruginosa can cause a wide array of chronic and acute infections associated with its ability to rapidly switch between planktonic, biofilm, and dispersed lifestyles, each with a specific arsenal for bacterial survival and virulence. At the cellular level, many of the physiological transitions are orchestrated by the intracellular second messenger c-di-GMP and its receptor-effector FleQ. A bacterial enhancer binding protein, FleQ acts as a master regulator of both flagellar motility and adherence factor secretion and uses remarkably different transcription activation mechanisms depending on its dinucleotide loading state, adenosine triphosphatase (ATPase) activity, interactions with polymerase sigma (sigma) factors, and complexation with a second ATPase, FleN. How the FleQ-FleN tandem can exert diverse effects through recognition of a conserved FleQ binding consensus has remained enigmatic. Here, we provide cryogenic electron microscopy (cryo-EM) structures of both c-di-GMP-bound and c-di-GMP-free FleQ-FleN complexes which deepen our understanding of the proteins' (di)nucleotide-dependent conformational switching and fine-tuned roles in gene expression regulation.

Structures of the P. aeruginosa FleQ-FleN master regulators reveal large-scale conformational switching in motility and biofilm control.,Torres-Sanchez L, Sana TG, Decossas M, Hashem Y, Krasteva PV Proc Natl Acad Sci U S A. 2023 Dec 12;120(50):e2312276120. doi: , 10.1073/pnas.2312276120. Epub 2023 Dec 5. PMID:38051770^[5]

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

References

↑ Dasgupta N, Ramphal R. Interaction of the antiactivator FleN with the transcriptional activator FleQ regulates flagellar number in Pseudomonas aeruginosa. J Bacteriol. 2001 Nov;183(22):6636-44. PMID:11673434 doi:10.1128/JB.183.22.6636-6644.2001
↑ Baraquet C, Murakami K, Parsek MR, Harwood CS. The FleQ protein from Pseudomonas aeruginosa functions as both a repressor and an activator to control gene expression from the pel operon promoter in response to c-di-GMP. Nucleic Acids Res. 2012 Aug;40(15):7207-18. PMID:22581773 doi:10.1093/nar/gks384
↑ Su T, Liu S, Wang K, Chi K, Zhu D, Wei T, Huang Y, Guo L, Hu W, Xu S, Lin Z, Gu L. The REC domain mediated dimerization is critical for FleQ from Pseudomonas aeruginosa to function as a c-di-GMP receptor and flagella gene regulator. J Struct Biol. 2015 Oct;192(1):1-13. doi: 10.1016/j.jsb.2015.09.002. Epub 2015, Sep 8. PMID:26362077 doi:http://dx.doi.org/10.1016/j.jsb.2015.09.002
↑ Arora SK, Ritchings BW, Almira EC, Lory S, Ramphal R. A transcriptional activator, FleQ, regulates mucin adhesion and flagellar gene expression in Pseudomonas aeruginosa in a cascade manner. J Bacteriol. 1997 Sep;179(17):5574-81. PMID:9287015 doi:10.1128/jb.179.17.5574-5581.1997
↑ Torres-Sánchez L, Sana TG, Decossas M, Hashem Y, Krasteva PV. Structures of the P. aeruginosa FleQ-FleN master regulators reveal large-scale conformational switching in motility and biofilm control. Proc Natl Acad Sci U S A. 2023 Dec 12;120(50):e2312276120. PMID:38051770 doi:10.1073/pnas.2312276120

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/8pb9"

Categories: Large Structures | Pseudomonas aeruginosa PAO1 | Krasteva PV | Torres-Sanchez LT

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8pb9 is ON HOLD  until Paper Publication
+==Cryo-EM structure of the c-di-GMP-bound FleQ-FleN master regulator complex from Pseudomonas aeruginosa==
+<StructureSection load='8pb9' size='340' side='right'caption='[[8pb9]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8pb9]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8PB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PB9 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.3&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=C2E:9,9-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d 3,2-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one)'>C2E</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=8pb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8pb9 OCA], [https://pdbe.org/8pb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8pb9 RCSB], [https://www.ebi.ac.uk/pdbsum/8pb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8pb9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FLEQ_PSEAE FLEQ_PSEAE] AAA+ ATPase enhancer-binding protein that acts as a transcription regulator and plays a role in the modulation of mucin adhesion and flagellar gene expression (PubMed:9287015, PubMed:11673434, PubMed:26362077). In addition to flagella genes, regulates also expression of biofilm-related genes (PubMed:22581773). Functions as a transcriptional repressor in the absence of c-di-GMP and as an activator when c-di-GMP is present (PubMed:22581773).<ref>PMID:11673434</ref> <ref>PMID:22581773</ref> <ref>PMID:26362077</ref> <ref>PMID:9287015</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Pseudomonas aeruginosa can cause a wide array of chronic and acute infections associated with its ability to rapidly switch between planktonic, biofilm, and dispersed lifestyles, each with a specific arsenal for bacterial survival and virulence. At the cellular level, many of the physiological transitions are orchestrated by the intracellular second messenger c-di-GMP and its receptor-effector FleQ. A bacterial enhancer binding protein, FleQ acts as a master regulator of both flagellar motility and adherence factor secretion and uses remarkably different transcription activation mechanisms depending on its dinucleotide loading state, adenosine triphosphatase (ATPase) activity, interactions with polymerase sigma (sigma) factors, and complexation with a second ATPase, FleN. How the FleQ-FleN tandem can exert diverse effects through recognition of a conserved FleQ binding consensus has remained enigmatic. Here, we provide cryogenic electron microscopy (cryo-EM) structures of both c-di-GMP-bound and c-di-GMP-free FleQ-FleN complexes which deepen our understanding of the proteins' (di)nucleotide-dependent conformational switching and fine-tuned roles in gene expression regulation.
-Authors:
+Structures of the P. aeruginosa FleQ-FleN master regulators reveal large-scale conformational switching in motility and biofilm control.,Torres-Sanchez L, Sana TG, Decossas M, Hashem Y, Krasteva PV Proc Natl Acad Sci U S A. 2023 Dec 12;120(50):e2312276120. doi: , 10.1073/pnas.2312276120. Epub 2023 Dec 5. PMID:38051770<ref>PMID:38051770</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8pb9" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Pseudomonas aeruginosa PAO1]]
+[[Category: Krasteva PV]]
+[[Category: Torres-Sanchez LT]]

8pb9

From Proteopedia

Revision as of 11:45, 13 December 2023

Cryo-EM structure of the c-di-GMP-bound FleQ-FleN master regulator complex from Pseudomonas aeruginosa

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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