4j40

</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=4j40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j40 OCA], [https://pdbe.org/4j40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j40 RCSB], [https://www.ebi.ac.uk/pdbsum/4j40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j40 ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Bacterial pathogenesis involves social behavior including biofilm formation and swarming, processes that are regulated by the bacterially unique second messenger cyclic di-GMP (c-di-GMP). Diguanylate cyclases containing GGDEF and phosphodiesterases containing EAL domains have been identified as the enzymes controlling cellular c-di-GMP levels, yet less is known regarding signal transmission and the targets of c-di-GMP. FimX, a protein from Pseudomonas aeruginosa that governs twitching motility, belongs to a large subfamily containing both GGDEF and EAL domains. Biochemical and structural analyses reveals its function as a high-affinity receptor for c-di-GMP. A model for full-length FimX was generated combining solution scattering data and crystal structures of the degenerate GGDEF and EAL domains. Although FimX forms a dimer in solution via the N-terminal domains, a crystallographic EAL domain dimer suggests modes for the regulation of FimX by c-di-GMP binding. The results provide the structural basis for c-di-GMP sensing via degenerate phosphodiesterases.

Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX.,Navarro MV, De N, Bae N, Wang Q, Sondermann H Structure. 2009 Aug 12;17(8):1104-16. PMID:19679088<ref>PMID:19679088</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 4j40" style="background-color:#fffaf0;"></div>

== References ==

<references/>