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| | <StructureSection load='7fir' size='340' side='right'caption='[[7fir]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='7fir' size='340' side='right'caption='[[7fir]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7fir]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FIR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7fir]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoanaerobacter_sp._X514 Thermoanaerobacter sp. X514]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7FIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7FIR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=GUP:ALPHA-L-GULOPYRANOSIDE'>GUP</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]] 2.2Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=Z2D:'>Z2D</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=GUP:ALPHA-L-GULOPYRANOSIDE'>GUP</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=Z2D:alpha-L-allopyranose'>Z2D</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-1,2-mannobiose_phosphorylase Beta-1,2-mannobiose phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.339 2.4.1.339] </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=7fir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fir OCA], [https://pdbe.org/7fir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fir RCSB], [https://www.ebi.ac.uk/pdbsum/7fir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fir ProSAT]</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=7fir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7fir OCA], [https://pdbe.org/7fir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7fir RCSB], [https://www.ebi.ac.uk/pdbsum/7fir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7fir ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/BMBP_THEPX BMBP_THEPX]] Probably involved in a salvage pathway for GDP-D-mannose biosynthesis (PubMed:25500577). Catalyzes the reversible phosphorolysis of 1,2-beta-oligomannan. In phosphorolytic reactions, prefers beta-1,2-mannobiose (beta-1,2-Man2) as substrate. Produces alpha-D-mannose 1-phosphate, which is the precursor of GDP-D-mannose (PubMed:25500577).<ref>PMID:25500577</ref>
| + | [https://www.uniprot.org/uniprot/BMBP_THEPX BMBP_THEPX] Probably involved in a salvage pathway for GDP-D-mannose biosynthesis (PubMed:25500577). Catalyzes the reversible phosphorolysis of 1,2-beta-oligomannan. In phosphorolytic reactions, prefers beta-1,2-mannobiose (beta-1,2-Man2) as substrate. Produces alpha-D-mannose 1-phosphate, which is the precursor of GDP-D-mannose (PubMed:25500577).<ref>PMID:25500577</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: Beta-1,2-mannobiose phosphorylase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chang, Z]] | + | [[Category: Thermoanaerobacter sp. X514]] |
| - | [[Category: Chen, C C]] | + | [[Category: Chang Z]] |
| - | [[Category: Dai, L]] | + | [[Category: Chen C-C]] |
| - | [[Category: Guo, R T]] | + | [[Category: Dai L]] |
| - | [[Category: Huang, J]] | + | [[Category: Guo R-T]] |
| - | [[Category: Liu, W]] | + | [[Category: Huang J]] |
| - | [[Category: Sun, Y]] | + | [[Category: Liu W]] |
| - | [[Category: Yang, J]] | + | [[Category: Sun Y]] |
| - | [[Category: Yang, Y]] | + | [[Category: Yang J]] |
| - | [[Category: Zhang, L]] | + | [[Category: Yang Y]] |
| - | [[Category: Complex structure]]
| + | [[Category: Zhang L]] |
| - | [[Category: Crystallization]]
| + | |
| - | [[Category: Mannobiose]]
| + | |
| - | [[Category: Phosphorylase]]
| + | |
| - | [[Category: Thermoanaerobacter]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
7fir is a 4 chain structure with sequence from Thermoanaerobacter sp. X514. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.2Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
BMBP_THEPX Probably involved in a salvage pathway for GDP-D-mannose biosynthesis (PubMed:25500577). Catalyzes the reversible phosphorolysis of 1,2-beta-oligomannan. In phosphorolytic reactions, prefers beta-1,2-mannobiose (beta-1,2-Man2) as substrate. Produces alpha-D-mannose 1-phosphate, which is the precursor of GDP-D-mannose (PubMed:25500577).[1]
Publication Abstract from PubMed
1,2-beta-Mannobiose phosphorylases (1,2-beta-MBPs) from glycoside hydrolase 130 (GH130) family are important bio-catalysts in glycochemistry applications owing to their ability in synthesizing oligomannans. Here, we report the crystal structure of a thermostable 1,2-beta-MBP from Thermoanaerobacter sp. X-514 termed Teth514_1789 to reveal the molecular basis of its higher thermostability and mechanism of action. We also solved the enzyme complexes of mannose, mannose-1-phosphate (M1P) and 1,4-beta-mannobiose to manifest the enzyme-substrate interaction networks of three main subsites. Notably, a Zn ion that should be derived from crystallization buffer was found in the active site and coordinates the phosphate moiety of M1P. Nonetheless, this Zn-coordination should reflect an inhibitory status as supplementing Zn severely impairs the enzyme activity. These results indicate that the effects of metal ions should be taken into consideration when applying Teth514_1789 and other related enzymes. Based on the structure, a reliable model of Teth514_1788 that shares 61.7% sequence identity to Teth514_1789 but displays a different substrate preference was built. Analyzing the structural features of these two closely related enzymes, we hypothesized that the length of a loop fragment that covers the entrance of the catalytic center might regulate the substrate selectivity. In conclusion, these information provide in-depth understanding of GH130 1,2-beta-MBPs and should serve as an important guidance for enzyme engineering for further applications.
Structural investigation of a thermostable 1,2-beta-mannobiose phosphorylase from Thermoanaerobacter sp. X-514.,Dai L, Chang Z, Yang J, Liu W, Yang Y, Chen CC, Zhang L, Huang JW, Sun Y, Guo RT Biochem Biophys Res Commun. 2021 Nov 19;579:54-61. doi:, 10.1016/j.bbrc.2021.09.046. Epub 2021 Sep 21. PMID:34587555[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chiku K, Nihira T, Suzuki E, Nishimoto M, Kitaoka M, Ohtsubo K, Nakai H. Discovery of two beta-1,2-mannoside phosphorylases showing different chain-length specificities from Thermoanaerobacter sp. X-514. PLoS One. 2014 Dec 12;9(12):e114882. doi: 10.1371/journal.pone.0114882., eCollection 2014. PMID:25500577 doi:http://dx.doi.org/10.1371/journal.pone.0114882
- ↑ Dai L, Chang Z, Yang J, Liu W, Yang Y, Chen CC, Zhang L, Huang JW, Sun Y, Guo RT. Structural investigation of a thermostable 1,2-beta-mannobiose phosphorylase from Thermoanaerobacter sp. X-514. Biochem Biophys Res Commun. 2021 Nov 19;579:54-61. doi:, 10.1016/j.bbrc.2021.09.046. Epub 2021 Sep 21. PMID:34587555 doi:http://dx.doi.org/10.1016/j.bbrc.2021.09.046
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