6ldq
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ldq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ldq OCA], [http://pdbe.org/6ldq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ldq RCSB], [http://www.ebi.ac.uk/pdbsum/6ldq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ldq 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=6ldq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ldq OCA], [http://pdbe.org/6ldq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ldq RCSB], [http://www.ebi.ac.uk/pdbsum/6ldq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ldq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In green species, sucrose can help antagonize abiotic stress. Sucrose phosphate synthase (SPS) is a well-known rate-limiting enzyme in the synthesis of sucrose. To date, however, there is no known crystal structure of SPS from plant or cyanobacteria. In this study, we report the first co-crystal structure of SPS from Thermosynechococcus elongatus with UDP and sucrose-6-phosphate (S6P). Within the catalytic site, the side chains of His158 and Glu331, along with two phosphate groups from UDP, form hydrogen bonds with the four hydroxyl groups of the glucose moiety in S6P. This association causes these four hydroxyl groups to become partially negatively charged, thus promoting formation of the C1 oxocarbenium ion. Breakage of the hydrogen bond between His158 and one of the hydroxyl groups may trigger covalent bond formation between the C1 oxocarbenium ion and the C2 hydroxyl of fructose-6-phosphate. Consistent with our structural model, we observed that two SPS mutants, H158A and E331A, lost all catalytic activity. Moreover, electron density of residues from two loops (loop1 and loop2) in the SPS A-domain was not observed, suggest their dynamic nature. B-factor analysis and molecular dynamics stimulations of the full-length enzyme and A-domain indicate that both loops are crucial for binding and release of substrate and product. In addition, temperature gradient analysis shows that SPS exhibits its highest activity at 70 degrees C, suggesting that this enzyme has the potential of being used in industrial production of S6P. | ||
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| + | Co-crystal Structure of Thermosynechococcus elongatus Sucrose Phosphate Synthase With UDP and Sucrose-6-Phosphate Provides Insight Into Its Mechanism of Action Involving an Oxocarbenium Ion and the Glycosidic Bond.,Li Y, Yao Y, Yang G, Tang J, Ayala GJ, Li X, Zhang W, Han Q, Yang T, Wang H, Mayo KH, Su J Front Microbiol. 2020 May 26;11:1050. doi: 10.3389/fmicb.2020.01050. eCollection , 2020. PMID:32528448<ref>PMID:32528448</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6ldq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:49, 25 June 2020
Sucrose-phosphate synthase (tll1590)_27_220_406_426_from Thermosynechococcus elongatus (twinned)
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