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7u1v
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7u1v is ON HOLD until Paper Publication Authors: Jacewicz, A., Sanchez, A.M., Shuman, S. Description: Structure of SPAC806.04c protein from fission...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of SPAC806.04c protein from fission yeast covalently bound to BeF3== | |
| + | <StructureSection load='7u1v' size='340' side='right'caption='[[7u1v]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7u1v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7U1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7U1V FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=7u1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7u1v OCA], [https://pdbe.org/7u1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7u1v RCSB], [https://www.ebi.ac.uk/pdbsum/7u1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7u1v ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ART1A_SCHPO ART1A_SCHPO] Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity).[UniProtKB:Q04371] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Domain of Unknown Function 89 (DUF89) proteins are metal-dependent phosphohydrolases. Exemplary DUF89 enzymes differ in their metal and phosphosubstrate preferences. Here, we interrogated the activities and structures of two DUF89 paralogs from fission yeast-Duf89 and Duf8901. We find that Duf89 and Duf8901 are cobalt/nickel-dependent phosphohydrolases adept at hydrolyzing p-nitrophenylphosphate and PP(i). Crystal structures of metal-free Duf89 and Co(2+)-bound Duf8901 disclosed two enzyme conformations that differed with respect to the position of a three-helix module, which is either oriented away from the active site in Duf89 or forms a lid over the active site in Duf8901. Lid closure results in a 16 A movement of Duf8901 Asp195, vis-a-vis Asp199 in Duf89, that brings Asp195 into contact with an octahedrally coordinated cobalt. Reaction of Duf8901 with BeCl(2) and NaF in the presence of divalent cations Co(2+), Ni(2+), or Zn(2+) generated covalent Duf8901-(Asp248)-beryllium trifluoride (BeF(3))*Co(2+), Duf8901-(Asp248)-BeF(3)*Ni(2+), or Duf8901-(Asp248)-BeF(3)*Zn(2+) adducts, the structures of which suggest a two-step catalytic mechanism via formation and hydrolysis of an enzyme-(aspartyl)-phosphate intermediate. Alanine mutations of Duf8901 Asp248, Asn249, Lys401, Asp286, and Asp195 that interact with BeF(3)*Co(2+) squelched p-nitrophenylphosphatase activity. A 1.8 A structure of a Duf8901-(Asp248)-AlF(4)-OH(2)*Co(2+) transition-state mimetic suggests an associative mechanism in which Asp195 and Asp363 orient and activate the water nucleophile. Whereas deletion of the duf89 gene elicited a phenotype in which expression of phosphate homeostasis gene pho1 was derepressed, deleting duf8901 did not, thereby hinting that the DUF89 paralogs have distinct functional repertoires in vivo. | ||
| - | + | Fission yeast Duf89 and Duf8901 are cobalt/nickel-dependent phosphatase-pyrophosphatases that act via a covalent aspartyl-phosphate intermediate.,Sanchez AM, Jacewicz A, Shuman S J Biol Chem. 2022 May;298(5):101851. doi: 10.1016/j.jbc.2022.101851. Epub 2022 , Mar 18. PMID:35314193<ref>PMID:35314193</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 7u1v" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Schizosaccharomyces pombe]] | ||
| + | [[Category: Jacewicz A]] | ||
| + | [[Category: Sanchez AM]] | ||
| + | [[Category: Shuman S]] | ||
Current revision
Structure of SPAC806.04c protein from fission yeast covalently bound to BeF3
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