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2v0n

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ACTIVATED RESPONSE REGULATOR PLED IN COMPLEX WITH C-DIGMP AND GTP- ALPHA-S

Structural highlights

2v0n is a 2 chain structure with sequence from Caulobacter vibrioides CB15. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.71Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PLED_CAUVN Response regulator that is part of a signal transduction pathway controlling cell differentiation in the swarmer-to-stalked cell transition.^[1] Catalyzes the condensation of two GTP molecules to the cyclic dinucleotide di-GMP (c-di-GMP), which acts as a secondary messenger.^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Cyclic di-guanosine monophosphate (c-di-GMP) is a ubiquitous bacterial second messenger involved in the regulation of cell surface-associated traits and persistence. We have determined the crystal structure of PleD from Caulobacter crescentus, a response regulator with a diguanylate cyclase (DGC) domain, in its activated form. The BeF(3)(-) modification of its receiver domain causes rearrangement with respect to an adaptor domain, which, in turn, promotes dimer formation, allowing for the efficient encounter of two symmetric catalytic domains. The substrate analog GTPalphaS and two putative cations are bound to the active sites in a manner similar to adenylate cyclases, suggesting an analogous two-metal catalytic mechanism. An allosteric c-di-GMP-binding mode that crosslinks DGC and an adaptor domain had been identified before. Here, a second mode is observed that crosslinks the DGC domains within a PleD dimer. Both modes cause noncompetitive product inhibition by domain immobilization.

Structure of BeF3- -modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition.,Wassmann P, Chan C, Paul R, Beck A, Heerklotz H, Jenal U, Schirmer T Structure. 2007 Aug;15(8):915-27. PMID:17697997^[3]

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

References

↑ Aldridge P, Paul R, Goymer P, Rainey P, Jenal U. Role of the GGDEF regulator PleD in polar development of Caulobacter crescentus. Mol Microbiol. 2003 Mar;47(6):1695-708. PMID:12622822 doi:10.1046/j.1365-2958.2003.03401.x
↑ Paul R, Weiser S, Amiot NC, Chan C, Schirmer T, Giese B, Jenal U. Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain. Genes Dev. 2004 Mar 15;18(6):715-27. PMID:15075296 doi:http://dx.doi.org/10.1101/gad.289504
↑ Wassmann P, Chan C, Paul R, Beck A, Heerklotz H, Jenal U, Schirmer T. Structure of BeF3- -modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition. Structure. 2007 Aug;15(8):915-27. PMID:17697997 doi:http://dx.doi.org/10.1016/j.str.2007.06.016

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2v0n"

Categories: Caulobacter vibrioides CB15 | Large Structures | Schirmer T | Wassmann P

@@ Line 3: / Line 3: @@
 <StructureSection load='2v0n' size='340' side='right'caption='[[2v0n]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2v0n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cauvc Cauvc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V0N FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2v0n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Caulobacter_vibrioides_CB15 Caulobacter vibrioides CB15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V0N FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAV:GUANOSINE-5-RP-ALPHA-THIO-TRIPHOSPHATE'>GAV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.71&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1w25|1w25]], [[2wb4|2wb4]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</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>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GAV:GUANOSINE-5-RP-ALPHA-THIO-TRIPHOSPHATE'>GAV</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2v0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0n OCA], [https://pdbe.org/2v0n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v0n RCSB], [https://www.ebi.ac.uk/pdbsum/2v0n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v0n ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PLED_CAUCR PLED_CAUCR]] Response regulator that is part of a signal transduction pathway controlling cell differentiation in the swarmer-to-stalked cell transition (By similarity).  Catalyzes the condensation of two GTP molecules to the cyclic dinucleotide di-GMP (c-di-GMP), which acts as a secondary messenger (By similarity).
+[https://www.uniprot.org/uniprot/PLED_CAUVN PLED_CAUVN] Response regulator that is part of a signal transduction pathway controlling cell differentiation in the swarmer-to-stalked cell transition.<ref>PMID:12622822</ref>   Catalyzes the condensation of two GTP molecules to the cyclic dinucleotide di-GMP (c-di-GMP), which acts as a secondary messenger.<ref>PMID:15075296</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Cauvc]]
+[[Category: Caulobacter vibrioides CB15]]
 [[Category: Large Structures]]
-[[Category: Schirmer, T]]
+[[Category: Schirmer T]]
-[[Category: Wassmann, P]]
+[[Category: Wassmann P]]
-[[Category: Allosteric product inhibition]]
-[[Category: Beryllium fluoride modification]]
-[[Category: Cell cycle]]
-[[Category: Lyase]]
-[[Category: Magnesium]]
-[[Category: Response regulator]]
-[[Category: Transducer]]
-[[Category: Two-component system]]

2v0n

From Proteopedia

Current revision

ACTIVATED RESPONSE REGULATOR PLED IN COMPLEX WITH C-DIGMP AND GTP- ALPHA-S

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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