|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==O-Acetyltransferase Domain of Pseudomonas putida AlgJ== | | ==O-Acetyltransferase Domain of Pseudomonas putida AlgJ== |
| - | <StructureSection load='4o8v' size='340' side='right' caption='[[4o8v]], [[Resolution|resolution]] 1.81Å' scene=''> | + | <StructureSection load='4o8v' size='340' side='right'caption='[[4o8v]], [[Resolution|resolution]] 1.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4o8v]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O8V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O8V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o8v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida_KT2440 Pseudomonas putida KT2440]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O8V FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4o8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o8v OCA], [http://pdbe.org/4o8v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o8v RCSB], [http://www.ebi.ac.uk/pdbsum/4o8v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o8v ProSAT]</span></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=4o8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o8v OCA], [https://pdbe.org/4o8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o8v RCSB], [https://www.ebi.ac.uk/pdbsum/4o8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o8v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ALGJ_PSEPK ALGJ_PSEPK]] Together with AlgI and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases the ability of alginate to act as a defense barrier (By similarity). | + | [https://www.uniprot.org/uniprot/ALGJ_PSEPK ALGJ_PSEPK] Together with AlgI and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases the ability of alginate to act as a defense barrier (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Howell, P L]] | + | [[Category: Large Structures]] |
| - | [[Category: Little, D J]] | + | [[Category: Pseudomonas putida KT2440]] |
| - | [[Category: Ricer, T]] | + | [[Category: Howell PL]] |
| - | [[Category: Robinson, H]] | + | [[Category: Little DJ]] |
| - | [[Category: Whitney, J C]] | + | [[Category: Ricer T]] |
| - | [[Category: Sgnh hydrolase-like]] | + | [[Category: Robinson H]] |
| - | [[Category: Transferase]] | + | [[Category: Whitney JC]] |
| Structural highlights
Function
ALGJ_PSEPK Together with AlgI and AlgF, forms an inner membrane complex which probably interacts with the alginate polymerization-transport complex and adds acetyl groups at the O-2 and O-3 positions of mannuronate residues. Acetylation of alginate is important for the architecture of biofilms and increases the ability of alginate to act as a defense barrier (By similarity).
Publication Abstract from PubMed
The O-acetylation of polysaccharides is a common modification used by pathogenic organisms to protect against external forces. Pseudomonas aeruginosa secretes the anionic, O-acetylated exopolysaccharide alginate during chronic infection in the lungs of cystic fibrosis patients to form the major constituent of a protective biofilm matrix. Four proteins have been implicated in the O-acetylation of alginate, AlgIJF and AlgX. To probe the biological function of AlgJ, we determined its structure to 1.83 A resolution. AlgJ is a SGNH hydrolase-like protein, which while structurally similar to the N-terminal domain of AlgX exhibits a distinctly different electrostatic surface potential. Consistent with other SGNH hydrolases, we identified a conserved catalytic triad composed of D190, H192 and S288 and demonstrated that AlgJ exhibits acetylesterase activity in vitro. Residues in the AlgJ signature motifs were found to form an extensive network of interactions that are critical for O-acetylation of alginate in vivo. Using two different electrospray ionization mass spectrometry (ESI-MS) assays we compared the abilities of AlgJ and AlgX to bind and acetylate alginate. Binding studies using defined length polymannuronic acid revealed that AlgJ exhibits either weak or no detectable polymer binding while AlgX binds polymannuronic acid specifically in a length-dependent manner. Additionally, AlgX was capable of utilizing the surrogate acetyl-donor 4-nitrophenyl acetate to catalyze the O-acetylation of polymannuronic acid. Our results, combined with previously published in vivo data, suggest that the annotated O-acetyltransferases AlgJ and AlgX have separate and distinct roles in O-acetylation. Our refined model for alginate acetylation places AlgX as the terminal acetlytransferase and provides a rationale for the variability in the number of proteins required for polysaccharide O-acetylation.
P. aeruginosa SGNH Hydrolase-Like Proteins AlgJ and AlgX Have Similar Topology but Separate and Distinct Roles in Alginate Acetylation.,Baker P, Ricer T, Moynihan PJ, Kitova EN, Walvoort MT, Little DJ, Whitney JC, Dawson K, Weadge JT, Robinson H, Ohman DE, Codee JD, Klassen JS, Clarke AJ, Howell PL PLoS Pathog. 2014 Aug 28;10(8):e1004334. doi: 10.1371/journal.ppat.1004334., eCollection 2014 Aug. PMID:25165982[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Baker P, Ricer T, Moynihan PJ, Kitova EN, Walvoort MT, Little DJ, Whitney JC, Dawson K, Weadge JT, Robinson H, Ohman DE, Codee JD, Klassen JS, Clarke AJ, Howell PL. P. aeruginosa SGNH Hydrolase-Like Proteins AlgJ and AlgX Have Similar Topology but Separate and Distinct Roles in Alginate Acetylation. PLoS Pathog. 2014 Aug 28;10(8):e1004334. doi: 10.1371/journal.ppat.1004334., eCollection 2014 Aug. PMID:25165982 doi:http://dx.doi.org/10.1371/journal.ppat.1004334
|
