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| | <StructureSection load='5evy' size='340' side='right'caption='[[5evy]], [[Resolution|resolution]] 2.47Å' scene=''> | | <StructureSection load='5evy' size='340' side='right'caption='[[5evy]], [[Resolution|resolution]] 2.47Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5evy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EVY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EVY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5evy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_putida Pseudomonas putida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EVY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SAL:2-HYDROXYBENZOIC+ACID'>SAL</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]] 2.47Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sal ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=303 "Bacillus fluorescens putidus" Flugge 1886])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SAL:2-HYDROXYBENZOIC+ACID'>SAL</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Salicylate_1-monooxygenase Salicylate 1-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.1 1.14.13.1] </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=5evy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5evy OCA], [https://pdbe.org/5evy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5evy RCSB], [https://www.ebi.ac.uk/pdbsum/5evy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5evy 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=5evy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5evy OCA], [http://pdbe.org/5evy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5evy RCSB], [http://www.ebi.ac.uk/pdbsum/5evy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5evy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q59713_PSEPU Q59713_PSEPU] |
| | <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: Bacillus fluorescens putidus flugge 1886]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Salicylate 1-monooxygenase]] | + | [[Category: Pseudomonas putida]] |
| - | [[Category: Morimoto, Y]] | + | [[Category: Morimoto Y]] |
| - | [[Category: Uemura, T]] | + | [[Category: Uemura T]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Monooxygenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
Q59713_PSEPU
Publication Abstract from PubMed
The X-ray crystal structure of a salicylate hydroxylase from Pseudomonas putida S-1 complexed with coenzyme FAD has been determined to a resolution of 2.5 A. Structural conservation with p- or m-hydroxybenzoate hydroxylase is very good throughout the topology, despite a low amino sequence identity of 20-40% between these three hydroxylases. Salicylate hydroxylase is composed of three distinct domains and includes FAD between domains I and II, which is accessible to solvent. In this study, which analyzes the tertiary structure of the enzyme, the unique reaction of salicylate, i.e. decarboxylative hydroxylation, and the structural roles of amino acids surrounding the substrate, are considered.
The catalytic mechanism of decarboxylative hydroxylation of salicylate hydroxylase revealed by crystal structure analysis at 2.5 A resolution.,Uemura T, Kita A, Watanabe Y, Adachi M, Kuroki R, Morimoto Y Biochem Biophys Res Commun. 2015 Nov 23. pii: S0006-291X(15)30956-6. doi:, 10.1016/j.bbrc.2015.11.087. PMID:26616054[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Uemura T, Kita A, Watanabe Y, Adachi M, Kuroki R, Morimoto Y. The catalytic mechanism of decarboxylative hydroxylation of salicylate hydroxylase revealed by crystal structure analysis at 2.5 A resolution. Biochem Biophys Res Commun. 2015 Nov 23. pii: S0006-291X(15)30956-6. doi:, 10.1016/j.bbrc.2015.11.087. PMID:26616054 doi:http://dx.doi.org/10.1016/j.bbrc.2015.11.087
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