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| | ==mouse SMP30/GNL== | | ==mouse SMP30/GNL== |
| - | <StructureSection load='4gn7' size='340' side='right' caption='[[4gn7]], [[Resolution|resolution]] 1.95Å' scene=''> | + | <StructureSection load='4gn7' size='340' side='right'caption='[[4gn7]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gn7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GN7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GN7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gn7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GN7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gn8|4gn8]], [[4gn9|4gn9]], [[4gna|4gna]], [[4gnb|4gnb]], [[4gnc|4gnc]]</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=4gn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gn7 OCA], [https://pdbe.org/4gn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gn7 RCSB], [https://www.ebi.ac.uk/pdbsum/4gn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gn7 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Smp30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Gluconolactonase Gluconolactonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.17 3.1.1.17] </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=4gn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gn7 OCA], [http://pdbe.org/4gn7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gn7 RCSB], [http://www.ebi.ac.uk/pdbsum/4gn7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gn7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/RGN_MOUSE RGN_MOUSE]] Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Catalyzes a key step in ascorbic acid (vitamin C) biosynthesis. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent cellular processes and enzyme activities (By similarity).<ref>PMID:16585534</ref> | + | [https://www.uniprot.org/uniprot/RGN_MOUSE RGN_MOUSE] Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Catalyzes a key step in ascorbic acid (vitamin C) biosynthesis. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent cellular processes and enzyme activities (By similarity).<ref>PMID:16585534</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: Gluconolactonase]] | + | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Aigaki, T]] | + | [[Category: Aigaki T]] |
| - | [[Category: Aizawa, S]] | + | [[Category: Aizawa S]] |
| - | [[Category: Harada, A]] | + | [[Category: Harada A]] |
| - | [[Category: Ishida, T]] | + | [[Category: Ishida T]] |
| - | [[Category: Ishigami, A]] | + | [[Category: Ishigami A]] |
| - | [[Category: Maruyama, N]] | + | [[Category: Maruyama N]] |
| - | [[Category: Senda, M]] | + | [[Category: Senda M]] |
| - | [[Category: Senda, T]] | + | [[Category: Senda T]] |
| - | [[Category: Beta propeller structure]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
RGN_MOUSE Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Catalyzes a key step in ascorbic acid (vitamin C) biosynthesis. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent cellular processes and enzyme activities (By similarity).[1]
Publication Abstract from PubMed
The senescence marker protein-30 (SMP30), which is also called regucalcin, exhibits gluconolactonase (GNL) activity. Biochemical and biological analyses revealed that SMP30/GNL catalyzes formation of the gamma-lactone-ring of L-gulonate in the ascorbic acid biosynthesis pathway. The molecular basis of the gamma-lactone formation, however, remains elusive due to the lack of structural information on SMP30/GNL in complex with its substrate. Here, we report the crystal structures of mouse SMP30/GNL and its complex with xylitol, a substrate analogue, and those with 1,5-anhydro-D-glucitol and D-glucose, product analogues. Comparison of the crystal structure of mouse SMP30/GNL with other related enzymes has revealed unique characteristics of mouse SMP30/GNL. First, the substrate-binding pocket of mouse SMP30/GNL is designed to specifically recognize monosaccharide molecules. The divalent metal ion in the active site and polar residues lining the substrate-binding cavity interact with hydroxyl groups of substrate/product analogues. Second, in mouse SMP30/GNL, a lid loop covering the substrate-binding cavity seems to hamper the binding of L-gulonate in an extended (or all-trans) conformation; L-gulonate seems to bind to the active site in a folded conformation. In contrast, the substrate-binding cavities of the other related enzymes are open to the solvent and do not have a cover. This structural feature of mouse SMP30/GNL seems to facilitate the gamma-lactone-ring formation.
Structural basis of the gamma-lactone-ring formation in ascorbic acid biosynthesis by the senescence marker protein-30/gluconolactonase.,Aizawa S, Senda M, Harada A, Maruyama N, Ishida T, Aigaki T, Ishigami A, Senda T PLoS One. 2013;8(1):e53706. doi: 10.1371/journal.pone.0053706. Epub 2013 Jan 22. PMID:23349732[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kondo Y, Inai Y, Sato Y, Handa S, Kubo S, Shimokado K, Goto S, Nishikimi M, Maruyama N, Ishigami A. Senescence marker protein 30 functions as gluconolactonase in L-ascorbic acid biosynthesis, and its knockout mice are prone to scurvy. Proc Natl Acad Sci U S A. 2006 Apr 11;103(15):5723-8. Epub 2006 Apr 3. PMID:16585534 doi:10.1073/pnas.0511225103
- ↑ Aizawa S, Senda M, Harada A, Maruyama N, Ishida T, Aigaki T, Ishigami A, Senda T. Structural basis of the gamma-lactone-ring formation in ascorbic acid biosynthesis by the senescence marker protein-30/gluconolactonase. PLoS One. 2013;8(1):e53706. doi: 10.1371/journal.pone.0053706. Epub 2013 Jan 22. PMID:23349732 doi:http://dx.doi.org/10.1371/journal.pone.0053706
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