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| | <StructureSection load='2r68' size='340' side='right'caption='[[2r68]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2r68' size='340' side='right'caption='[[2r68]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2r68]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloh Haloh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R68 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2r68]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halothermothrix_orenii_H_168 Halothermothrix orenii H 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R68 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2r66|2r66]], [[2r60|2r60]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F6P:FRUCTOSE-6-PHOSPHATE'>F6P</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900057:sucrose-6-phosphate'>PRD_900057</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=373903 HALOH])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Sucrose-phosphate_synthase Sucrose-phosphate synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.14 2.4.1.14] </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=2r68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r68 OCA], [https://pdbe.org/2r68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r68 RCSB], [https://www.ebi.ac.uk/pdbsum/2r68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r68 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=2r68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r68 OCA], [https://pdbe.org/2r68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r68 RCSB], [https://www.ebi.ac.uk/pdbsum/2r68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r68 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B8CZ51_HALOH B8CZ51_HALOH] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Haloh]] | + | [[Category: Halothermothrix orenii H 168]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Sucrose-phosphate synthase]]
| + | [[Category: Chua TK]] |
| - | [[Category: Chua, T K]] | + | [[Category: Sivaraman J]] |
| - | [[Category: Sivaraman, J]] | + | |
| - | [[Category: Rossmann-fold]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
B8CZ51_HALOH
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Sucrose phosphate synthase (SPS) catalyzes the transfer of a glycosyl group from an activated donor sugar, such as uridine diphosphate glucose (UDP-Glc), to a saccharide acceptor D-fructose 6-phosphate (F6P), resulting in the formation of UDP and D-sucrose-6'-phosphate (S6P). This is a central regulatory process in the production of sucrose in plants, cyanobacteria, and proteobacteria. Here, we report the crystal structure of SPS from the nonphotosynthetic bacterium Halothermothrix orenii and its complexes with the substrate F6P and the product S6P. SPS has two distinct Rossmann-fold domains with a large substrate binding cleft at the interdomain interface. Structures of two complexes show that both the substrate F6P and the product S6P bind to the A-domain of SPS. Based on comparative analysis of the SPS structure with other related enzymes, the donor substrate, nucleotide diphosphate glucose, binds to the B-domain of SPS. Furthermore, we propose a mechanism of catalysis by H. orenii SPS. Our findings indicate that SPS from H. orenii may represent a valid model for the catalytic domain of plant SPSs and thus may provide useful insight into the reaction mechanism of the plant enzyme.
The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and binding mode.,Chua TK, Bujnicki JM, Tan TC, Huynh F, Patel BK, Sivaraman J Plant Cell. 2008 Apr;20(4):1059-72. Epub 2008 Apr 18. PMID:18424616[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chua TK, Bujnicki JM, Tan TC, Huynh F, Patel BK, Sivaraman J. The structure of sucrose phosphate synthase from Halothermothrix orenii reveals its mechanism of action and binding mode. Plant Cell. 2008 Apr;20(4):1059-72. Epub 2008 Apr 18. PMID:18424616 doi:10.1105/tpc.107.051193
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