View source for 7a7e


==Structure of a delta-N mutant - E232start - of PA1120 (TpbB or YfiN) from Pseudomonas aeruginosa (PAO1) comprising only the GGDEF domain==
<StructureSection load='7a7e' size='340' side='right'caption='[[7a7e]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7a7e]] is a 3 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=7A7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A7E FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a7e OCA], [https://pdbe.org/7a7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a7e RCSB], [https://www.ebi.ac.uk/pdbsum/7a7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a7e ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9I4L5_PSEAE Q9I4L5_PSEAE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
GGDEF-containing proteins respond to different environmental cues to finely modulate cyclic diguanylate (c-di-GMP) levels in time and space, making the allosteric control a distinctive trait of the corresponding proteins. The diguanylate cyclase mechanism is emblematic of this control: two GGDEF domains, each binding one GTP molecule, must dimerize to enter catalysis and yield c-di-GMP. The need for dimerization makes the GGDEF domain an ideal conformational switch in multidomain proteins. A re-evaluation of the kinetic profile of previously characterized GGDEF domains indicated that they are also able to convert GTP to GMP: this unexpected reactivity occurs when conformational issues hamper the cyclase activity. These results create new questions regarding the characterization and engineering of these proteins for in solution or structural studies.

Studying GGDEF Domain in the Act: Minimize Conformational Frustration to Prevent Artefacts.,Mantoni F, Scribani Rossi C, Paiardini A, Di Matteo A, Cappellacci L, Petrelli R, Ricciutelli M, Paone A, Cutruzzola F, Giardina G, Rinaldo S Life (Basel). 2021 Jan 6;11(1). pii: life11010031. doi: 10.3390/life11010031. PMID:33418960<ref>PMID:33418960</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7a7e" style="background-color:#fffaf0;"></div>

==See Also==
*[[Diguanylate cyclase|Diguanylate cyclase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas aeruginosa PAO1]]
[[Category: Brunotti P]]
[[Category: Giardina G]]
[[Category: Mantoni F]]
[[Category: Rinaldo S]]