2l74

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==Solution structure of the PilZ domain protein PA4608 complex with c-di-GMP identifies charge clustering as molecular readout==
==Solution structure of the PilZ domain protein PA4608 complex with c-di-GMP identifies charge clustering as molecular readout==
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<StructureSection load='2l74' size='340' side='right'caption='[[2l74]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2l74' size='340' side='right'caption='[[2l74]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2l74]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L74 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2l74]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L74 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L74 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ywu|1ywu]], [[3kyf|3kyf]]</div></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=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>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA4608 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</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=2l74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l74 OCA], [https://pdbe.org/2l74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l74 RCSB], [https://www.ebi.ac.uk/pdbsum/2l74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l74 ProSAT]</span></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=2l74 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l74 OCA], [https://pdbe.org/2l74 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l74 RCSB], [https://www.ebi.ac.uk/pdbsum/2l74 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l74 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CDGBP_PSEAE CDGBP_PSEAE]] Binds the second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP). Can bind two c-di-GMP molecules per monomer. May play a role in bacterial second-messenger regulated processes. Binding to c-di-GMP induces a conformational change of the C- and N-termini resulting in the exposure of a highly negative surface on one side of the protein to a possible effector protein.<ref>PMID:17096419</ref> <ref>PMID:21280119</ref> <ref>PMID:21310957</ref>
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[https://www.uniprot.org/uniprot/CDGBP_PSEAE CDGBP_PSEAE] Binds the second messenger bis-(3'-5') cyclic dimeric guanosine monophosphate (c-di-GMP). Can bind two c-di-GMP molecules per monomer. May play a role in bacterial second-messenger regulated processes. Binding to c-di-GMP induces a conformational change of the C- and N-termini resulting in the exposure of a highly negative surface on one side of the protein to a possible effector protein.<ref>PMID:17096419</ref> <ref>PMID:21280119</ref> <ref>PMID:21310957</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cyclic di-guanosine monophosphate (c-di-GMP) is a ubiquitous bacterial second messenger that controls the switch from a single-cell lifestyle to surface-attached, multicellular communities called biofilms. PilZ domain proteins are a family of bacterial c-di-GMP receptors, which control various cellular processes. We have solved the solution structure of the Pseudomonas aeruginosa single-domain PilZ protein PA4608 in complex with c-di-GMP by NMR spectroscopy. Isotope labeling by 13C and 15N of both the ligand and the protein made it possible to define the structure of c-di-GMP in the complex at high precision by a large number of intermolecular and intraligand NOEs and by two intermolecular hydrogen bond scalar couplings. Complex formation induces significant rearrangements of the C- and N-terminal parts of PA4608. C-di-GMP binds as an intercalated, symmetric dimer to one side of the beta-barrel thereby displacing the C-terminal helix of the apo state. The N-terminal RxxxR PilZ domain motif, which is flexible in the apo state, wraps around the ligand and in turn ties the displaced C-terminus in a loose manner by a number of hydrophic contacts. The recognition of the dimeric ligand is achieved by numerous H-bonds and stacking interactions involving residues R8, R9, R10, R13 of the PilZ motif, as well as beta-barrel residues D35 and W77. As a result of the rearrangement of the N- and C-termini, a highly negative surface is created on one side of the protein complex. We propose that the movement of the termini and the resulting negative surface forms the basis for downstream signaling.
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Solution structure of the PilZ domain protein PA4608 complex with c-di-GMP identifies charge clustering as molecular readout.,Habazettl J, Allan MG, Jenal U, Grzesiek S J Biol Chem. 2011 Feb 10. PMID:21310957<ref>PMID:21310957</ref>
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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 2l74" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Allan, M]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Grzesiek, S]]
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[[Category: Allan M]]
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[[Category: Habazettl, J]]
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[[Category: Grzesiek S]]
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[[Category: Jenal, U]]
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[[Category: Habazettl J]]
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[[Category: C-di-gmp]]
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[[Category: Jenal U]]
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[[Category: C-di-gmp binding protein]]
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[[Category: Pa4608]]
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[[Category: Pilz]]
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[[Category: Unknown function]]
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Current revision

Solution structure of the PilZ domain protein PA4608 complex with c-di-GMP identifies charge clustering as molecular readout

PDB ID 2l74

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