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| | <StructureSection load='5tka' size='340' side='right'caption='[[5tka]], [[Resolution|resolution]] 2.05Å' scene=''> | | <StructureSection load='5tka' size='340' side='right'caption='[[5tka]], [[Resolution|resolution]] 2.05Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5tka]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TKA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TKA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5tka]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_megaterium Priestia megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TKA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TKA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.048Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tk6|5tk6]], [[5tk7|5tk7]], [[5tk8|5tk8]], [[5tk9|5tk9]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">oxsA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</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=5tka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tka OCA], [https://pdbe.org/5tka PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tka RCSB], [https://www.ebi.ac.uk/pdbsum/5tka PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tka 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=5tka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tka OCA], [http://pdbe.org/5tka PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tka RCSB], [http://www.ebi.ac.uk/pdbsum/5tka PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tka ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O24769_PRIMG O24769_PRIMG] |
| | <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: Atcc 14581]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bridwell-Rabb, J]] | + | [[Category: Priestia megaterium]] |
| - | [[Category: Drennan, C L]] | + | [[Category: Bridwell-Rabb J]] |
| - | [[Category: Hd-domain phosphohydrolase]]
| + | [[Category: Drennan CL]] |
| - | [[Category: Metal binding protein]] | + | |
| - | [[Category: Metalloprotein]]
| + | |
| - | [[Category: Oxetanocin]]
| + | |
| Structural highlights
Function
O24769_PRIMG
Publication Abstract from PubMed
HD domain phosphohydrolase enzymes are characterized by a conserved set of histidine and aspartate residues that coordinate an active site metallocenter. Despite the important roles these enzymes play in nucleotide metabolism and signal transduction, few have been both biochemically and structurally characterized. Here, we present X-ray crystal structures and biochemical characterization of the Bacillus megaterium HD domain phosphohydrolase OxsA, involved in the biosynthesis of the antitumor, antiviral, and antibacterial compound oxetanocin-A. These studies reveal a previously uncharacterized reaction for this family; OxsA catalyzes the conversion of a triphosphorylated compound into a nucleoside, releasing one molecule of inorganic phosphate at a time. Remarkably, this functionality is a result of the OxsA active site, which based on structural and kinetic analyses has been tailored to bind the small, four-membered ring of oxetanocin-A over larger substrates. Furthermore, our OxsA structures show an active site that switches from a dinuclear to a mononuclear metal center as phosphates are eliminated from substrate.
An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis.,Bridwell-Rabb J, Kang G, Zhong A, Liu HW, Drennan CL Proc Natl Acad Sci U S A. 2016 Nov 29;113(48):13750-13755. Epub 2016 Nov 14. PMID:27849620[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bridwell-Rabb J, Kang G, Zhong A, Liu HW, Drennan CL. An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis. Proc Natl Acad Sci U S A. 2016 Nov 29;113(48):13750-13755. Epub 2016 Nov 14. PMID:27849620 doi:http://dx.doi.org/10.1073/pnas.1613610113
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