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| | <StructureSection load='6umr' size='340' side='right'caption='[[6umr]], [[Resolution|resolution]] 2.21Å' scene=''> | | <StructureSection load='6umr' size='340' side='right'caption='[[6umr]], [[Resolution|resolution]] 2.21Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6umr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UMR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UMR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6umr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UMR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 2.21Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6umq|6umq]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARMT1, C6orf211 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6umr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6umr OCA], [https://pdbe.org/6umr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6umr RCSB], [https://www.ebi.ac.uk/pdbsum/6umr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6umr ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6umr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6umr OCA], [http://pdbe.org/6umr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6umr RCSB], [http://www.ebi.ac.uk/pdbsum/6umr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6umr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ARMT1_HUMAN ARMT1_HUMAN]] 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). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues (PubMed:25732820). Possibly methylates PCNA, suggesting it is involved in the DNA damage response (PubMed:25732820).[UniProtKB:Q04371]<ref>PMID:25732820</ref> | + | [https://www.uniprot.org/uniprot/ARMT1_HUMAN ARMT1_HUMAN] 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). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues (PubMed:25732820). Possibly methylates PCNA, suggesting it is involved in the DNA damage response (PubMed:25732820).[UniProtKB:Q04371]<ref>PMID:25732820</ref> |
| | <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: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dennis, T N]] | + | [[Category: Dennis TN]] |
| - | [[Category: Kenjic, N]] | + | [[Category: Kenjic N]] |
| - | [[Category: Perry, J J]] | + | [[Category: Perry JJ]] |
| - | [[Category: Duf89]]
| + | |
| - | [[Category: Metabolite repair]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
ARMT1_HUMAN 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). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues (PubMed:25732820). Possibly methylates PCNA, suggesting it is involved in the DNA damage response (PubMed:25732820).[UniProtKB:Q04371][1]
Publication Abstract from PubMed
Metabolite damage control is a critical but poorly defined aspect of cellular biochemistry, which likely involves many of the so far functionally uncharacterized protein domain (domains of unknown function; DUFs). We have determined the crystal structure of the human DUF89 protein product of the C6ORF211 gene to 1.85 A. The crystal structure shows that the protein contains a core alpha-beta-alpha fold with an active site-bound metal ion and alpha-helical bundle N-terminal cap, which are both conserved features of subfamily III DUF89 domains. The biochemical activities of the human protein are conserved with those of a previously characterized budding yeast homolog, where an in vitro phosphatase activity is supported by divalent cations that include Co(2+), Ni(2+), Mn(2+) or Mg(2+). Full steady-state kinetics parameters of human DUF89 using a standard PNPP phosphatase assay revealed a six times higher catalytic efficiency in presence of Co(2+) compared to Mg(2+). The human enzyme targets a number of phosphate substrates similar to the budding yeast homolog, while it lacks a previously indicated methyltransferase activity. The highest activity on substrate was observed with fructose-1-phosphate, a potent glycating agent, and thus human DUF89 phosphatase activity may also play a role in limiting the buildup of phospho-glycan species and their related damaged metabolites.
Human ARMT1 structure and substrate specificity indicates that it is a DUF89 family damage-control phosphatase.,Dennis TN, Kenjic N, Kang AS, Lowenson JD, Kirkwood JS, Clarke SG, Jefferson P Perry J J Struct Biol. 2020 Jul 15:107576. doi: 10.1016/j.jsb.2020.107576. PMID:32682077[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Perry JJ, Ballard GD, Albert AE, Dobrolecki LE, Malkas LH, Hoelz DJ. Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase that targets PCNA and is linked to the DNA damage response. Cell Rep. 2015 Mar 3;10(8):1288-96. doi: 10.1016/j.celrep.2015.01.054. Epub 2015 , Feb 26. PMID:25732820 doi:http://dx.doi.org/10.1016/j.celrep.2015.01.054
- ↑ Dennis TN, Kenjic N, Kang AS, Lowenson JD, Kirkwood JS, Clarke SG, Jefferson P Perry J. Human ARMT1 structure and substrate specificity indicates that it is a DUF89 family damage-control phosphatase. J Struct Biol. 2020 Jul 15:107576. doi: 10.1016/j.jsb.2020.107576. PMID:32682077 doi:http://dx.doi.org/10.1016/j.jsb.2020.107576
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