2r60
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2r60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halothermothrix_orenii Halothermothrix orenii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R60 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2r60]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halothermothrix_orenii Halothermothrix orenii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R60 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2R60 FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2r60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r60 OCA], [https://pdbe.org/2r60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r60 RCSB], [https://www.ebi.ac.uk/pdbsum/2r60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r60 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=2r60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r60 OCA], [https://pdbe.org/2r60 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2r60 RCSB], [https://www.ebi.ac.uk/pdbsum/2r60 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2r60 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/B2CCB8_9FIRM B2CCB8_9FIRM] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2r60 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2r60 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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. | ||
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| - | 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<ref>PMID:18424616</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2r60" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Halothermothrix orenii]] | [[Category: Halothermothrix orenii]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Chua TK]] | |
| - | [[Category: Chua | + | [[Category: Sivaraman J]] |
| - | [[Category: Sivaraman | + | |
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Current revision
Structure of apo Sucrose Phosphate Synthase (SPS) of Halothermothrix orenii
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