8bc2
From Proteopedia
(Difference between revisions)
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<StructureSection load='8bc2' size='340' side='right'caption='[[8bc2]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='8bc2' size='340' side='right'caption='[[8bc2]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[8bc2]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[8bc2]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Priestia_aryabhattai Priestia aryabhattai]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BC2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BC2 FirstGlance]. <br> |
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6Å</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=8bc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bc2 OCA], [https://pdbe.org/8bc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bc2 RCSB], [https://www.ebi.ac.uk/pdbsum/8bc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bc2 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=8bc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bc2 OCA], [https://pdbe.org/8bc2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bc2 RCSB], [https://www.ebi.ac.uk/pdbsum/8bc2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bc2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | [https://www.uniprot.org/uniprot/ | + | [https://www.uniprot.org/uniprot/SFTAL_PRIM1 SFTAL_PRIM1] Part of the sulfo-TAL (or sulfo-SFT) pathway, a D-sulfoquinovose degradation pathway that produces sulfolactate (SL) (PubMed:33036753). Catalyzes the conversion of 6-deoxy-6-sulfo-D-fructose (SF) and glyceraldehyde 3-phosphate (GAP) into fructose-6-phosphate (F6P) and 3-sulfolactaldehyde (SLA) (PubMed:33036753, PubMed:36805128). Can also catalyze the SF-cleavage with erythrose 4-phosphate (E4P) as acceptor, forming 3-sulfolactaldehyde (SLA) and sedoheptulose 7-phosphate (S7P) (PubMed:36805128).<ref>PMID:33036753</ref> <ref>PMID:36805128</ref> |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Sulfoquinovose (SQ) is a key component of plant sulfolipids (sulfoquinovosyl diacylglycerols) and a major environmental reservoir of biological sulfur. Breakdown of SQ is achieved by bacteria through the pathways of sulfoglycolysis. The sulfoglycolytic sulfofructose transaldolase (sulfo-SFT) pathway is used by gut-resident firmicutes and soil saprophytes. After isomerization of SQ to sulfofructose (SF), the namesake enzyme catalyzes the transaldol reaction of SF transferring dihydroxyacetone to 3C/4C acceptors to give sulfolactaldehyde and fructose-6-phosphate or sedoheptulose-7-phosphate. We report the 3D cryo-EM structure of SF transaldolase from Bacillus megaterium in apo and ligand bound forms, revealing a decameric structure formed from two pentameric rings of the protomer. We demonstrate a covalent "Schiff base" intermediate formed by reaction of SF with Lys89 within a conserved Asp-Lys-Glu catalytic triad and defined by an Arg-Trp-Arg sulfonate recognition triad. The structural characterization of the signature enzyme of the sulfo-SFT pathway provides key insights into molecular recognition of the sulfonate group of sulfosugars. | ||
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| + | Structure and mechanism of sulfofructose transaldolase, a key enzyme in sulfoquinovose metabolism.,Snow AJD, Sharma M, Abayakoon P, Williams SJ, Blaza JN, Davies GJ Structure. 2023 Mar 2;31(3):244-252.e4. doi: 10.1016/j.str.2023.01.010. Epub 2023 , Feb 17. PMID:36805128<ref>PMID:36805128</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 8bc2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Priestia | + | [[Category: Priestia aryabhattai]] |
[[Category: Blaza J]] | [[Category: Blaza J]] | ||
[[Category: Davies GJ]] | [[Category: Davies GJ]] | ||
[[Category: Sharma M]] | [[Category: Sharma M]] | ||
[[Category: Snow AJD]] | [[Category: Snow AJD]] | ||
Current revision
Ligand-Free Structure of the decameric sulfofructose transaldolase BmSF-TAL
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