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[[ | ==Crystal structure of the FimX EAL domain in complex with reaction product pGpG== | ||
<StructureSection load='4afy' size='340' side='right' caption='[[4afy]], [[Resolution|resolution]] 2.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4afy]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AFY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AFY FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PA4959 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cyclic-guanylate-specific_phosphodiesterase Cyclic-guanylate-specific phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.52 3.1.4.52] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4afy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4afy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4afy RCSB], [http://www.ebi.ac.uk/pdbsum/4afy PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
FimX is a large multidomain protein containing an EAL domain and involved in twitching motility in Pseudomonas aeruginosa. We present here two crystallographic structures of the EAL domain of FimX (residues 438-686): one of the apo form and the other of a complex with 5'-pGpG, the reaction product of the hydrolysis of c-di-GMP. In both crystal forms, the EAL domains form a dimer delimiting a large cavity encompassing the catalytic pockets. The ligand is trapped in this cavity by its sugar phosphate moiety. We confirmed by NMR that the guanine bases are not involved in the interaction in solution. We solved here the first structure of an EAL domain bound to the reaction product 5'-pGpG. Though isolated FimX EAL domain has a very low catalytic activity, which would not be significant compared to other catalytic EAL domains, the structure with the product of the reaction can provides some hints in the mechanism of hydrolysis of the c-di-GMP by EAL domains. | |||
Crystal Structure of an EAL Domain in Complex with Reaction Product 5'-pGpG.,Robert-Paganin J, Nonin-Lecomte S, Rety S PLoS One. 2012;7(12):e52424. doi: 10.1371/journal.pone.0052424. Epub 2012 Dec 20. PMID:23285035<ref>PMID:23285035</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Cyclic-guanylate-specific phosphodiesterase]] | [[Category: Cyclic-guanylate-specific phosphodiesterase]] | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Nonin-Lecomte, S | [[Category: Nonin-Lecomte, S]] | ||
[[Category: Rety, S | [[Category: Rety, S]] | ||
[[Category: Robert-Paganin, J | [[Category: Robert-Paganin, J]] | ||
[[Category: Cdigmp biofilm]] | [[Category: Cdigmp biofilm]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Phosphodiesterase]] | [[Category: Phosphodiesterase]] | ||
Revision as of 13:52, 4 January 2015
Crystal structure of the FimX EAL domain in complex with reaction product pGpGCrystal structure of the FimX EAL domain in complex with reaction product pGpG
Structural highlights
Publication Abstract from PubMedFimX is a large multidomain protein containing an EAL domain and involved in twitching motility in Pseudomonas aeruginosa. We present here two crystallographic structures of the EAL domain of FimX (residues 438-686): one of the apo form and the other of a complex with 5'-pGpG, the reaction product of the hydrolysis of c-di-GMP. In both crystal forms, the EAL domains form a dimer delimiting a large cavity encompassing the catalytic pockets. The ligand is trapped in this cavity by its sugar phosphate moiety. We confirmed by NMR that the guanine bases are not involved in the interaction in solution. We solved here the first structure of an EAL domain bound to the reaction product 5'-pGpG. Though isolated FimX EAL domain has a very low catalytic activity, which would not be significant compared to other catalytic EAL domains, the structure with the product of the reaction can provides some hints in the mechanism of hydrolysis of the c-di-GMP by EAL domains. Crystal Structure of an EAL Domain in Complex with Reaction Product 5'-pGpG.,Robert-Paganin J, Nonin-Lecomte S, Rety S PLoS One. 2012;7(12):e52424. doi: 10.1371/journal.pone.0052424. Epub 2012 Dec 20. PMID:23285035[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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