Crystal structure of an EAL domain in complex with reaction product 5'-pGpG
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 prod...
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| Veröffentlicht in: | PloS one 2012-12, Vol.7 (12), p.e52424-e52424 |
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| creator | Robert-Paganin, Julien Nonin-Lecomte, Sylvie Réty, Stéphane |
| description | 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. |
| doi_str_mv | 10.1371/journal.pone.0052424 |
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This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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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. 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Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Robert-Paganin, Julien</au><au>Nonin-Lecomte, Sylvie</au><au>Réty, Stéphane</au><au>Dobson, Renwick</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of an EAL domain in complex with reaction product 5'-pGpG</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2012-12-20</date><risdate>2012</risdate><volume>7</volume><issue>12</issue><spage>e52424</spage><epage>e52424</epage><pages>e52424-e52424</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>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.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>23285035</pmid><doi>10.1371/journal.pone.0052424</doi><tpages>e52424</tpages><orcidid>https://orcid.org/0000-0001-5155-8088</orcidid><orcidid>https://orcid.org/0000-0002-2089-6727</orcidid><orcidid>https://orcid.org/0000-0001-6102-2025</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Apoproteins - chemistry Apoproteins - metabolism Bacterial Proteins - chemistry Bacterial Proteins - metabolism Biochemistry, Molecular Biology Biofilms Biology Biosynthesis Catalysis Catalytic activity Catalytic Domain Crystal structure Crystallography Crystallography, X-Ray Cyclic GMP - analogs & derivatives Cyclic GMP - metabolism Deoxyguanine Nucleotides - metabolism Guanine Hydrolysis Life Sciences Ligands Magnesium - metabolism Models, Molecular Molecular Sequence Data Motility Nitrophenols - metabolism NMR Nuclear magnetic resonance Phosphates Phosphoric Diester Hydrolases - metabolism Physics Protein Binding Protein Multimerization Protein Structure, Tertiary Proteins Pseudomonas aeruginosa Pseudomonas aeruginosa - enzymology Purines Sequence Alignment Signal transduction Solutions Structural Biology Studies Sugar Twitching |
| title | Crystal structure of an EAL domain in complex with reaction product 5'-pGpG |
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