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| | ==Chromosomal trehalose-6-phosphate phosphatase from P. aeruginosa== | | ==Chromosomal trehalose-6-phosphate phosphatase from P. aeruginosa== |
| - | <StructureSection load='6d3w' size='340' side='right' caption='[[6d3w]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='6d3w' size='340' side='right'caption='[[6d3w]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6d3w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp._hmsc75e02 Pseudomonas sp. hmsc75e02]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D3W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6D3W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6d3w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._HMSC75E02 Pseudomonas sp. HMSC75E02]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6D3W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6D3W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6cj0|6cj0]], [[6d3v|6d3v]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMPREF3289_15950 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1608908 Pseudomonas sp. HMSC75E02])</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=6d3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d3w OCA], [https://pdbe.org/6d3w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6d3w RCSB], [https://www.ebi.ac.uk/pdbsum/6d3w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6d3w ProSAT]</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=6d3w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6d3w OCA], [http://pdbe.org/6d3w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6d3w RCSB], [http://www.ebi.ac.uk/pdbsum/6d3w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6d3w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A1S1GKD7_9PSED A0A1S1GKD7_9PSED] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pseudomonas sp. hmsc75e02]] | + | [[Category: Large Structures]] |
| - | [[Category: Cross, M]] | + | [[Category: Pseudomonas sp. HMSC75E02]] |
| - | [[Category: Hofmann, A]] | + | [[Category: Cross M]] |
| - | [[Category: Park, S Y]] | + | [[Category: Hofmann A]] |
| - | [[Category: Had superfamily/rossmann fold]]
| + | [[Category: Park S-Y]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Phosphohydrolase]]
| + | |
| - | [[Category: Trehalose-6-phosphate]]
| + | |
| Structural highlights
Function
A0A1S1GKD7_9PSED
Publication Abstract from PubMed
The opportunistic bacterium Pseudomonas aeruginosa has been recognized as an important pathogen of clinical relevance and is a leading cause of hospital-acquired infections. The presence of a glycolytic enzyme in Pseudomonas, which is known to be inhibited by trehalose 6-phosphate (T6P) in other organisms, suggests that these bacteria may be vulnerable to the detrimental effects of intracellular T6P accumulation. In the present study, we explored the structural and functional properties of trehalose 6-phosphate phosphatase (TPP) in P. aeruginosa in support of future target-based drug discovery. A survey of genomes revealed the existence of 2 TPP genes with either chromosomal or extrachromosomal location. Both TPPs were produced as recombinant proteins, and characterization of their enzymatic properties confirmed specific, magnesium-dependent catalytic hydrolysis of T6P. The 3-dimensional crystal structure of the chromosomal TPP revealed a protein dimer arising through beta-sheet expansion of the individual monomers, which possess the overall fold of halo-acid dehydrogenases.-Cross, M., Biberacher, S., Park, S.-Y., Rajan, S., Korhonen, P., Gasser, R. B., Kim, J.-S., Coster, M. J., Hofmann, A. Trehalose 6-phosphate phosphatases of Pseudomonas aeruginosa.
Trehalose 6-phosphate phosphatases of Pseudomonas aeruginosa.,Cross M, Biberacher S, Park SY, Rajan S, Korhonen P, Gasser RB, Kim JS, Coster MJ, Hofmann A FASEB J. 2018 Apr 24:fj201800500R. doi: 10.1096/fj.201800500R. PMID:29688811[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cross M, Biberacher S, Park SY, Rajan S, Korhonen P, Gasser RB, Kim JS, Coster MJ, Hofmann A. Trehalose 6-phosphate phosphatases of Pseudomonas aeruginosa. FASEB J. 2018 Apr 24:fj201800500R. doi: 10.1096/fj.201800500R. PMID:29688811 doi:http://dx.doi.org/10.1096/fj.201800500R
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