8bc2

From Proteopedia

(Difference between revisions)

Current revision

Ligand-Free Structure of the decameric sulfofructose transaldolase BmSF-TAL

Structural highlights

8bc2 is a 10 chain structure with sequence from Priestia aryabhattai. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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).^[1] ^[2]

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.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Liu Y, Wei Y, Zhou Y, Ang EL, Zhao H, Zhang Y. A transaldolase-dependent sulfoglycolysis pathway in Bacillus megaterium DSM 1804. Biochem Biophys Res Commun. 2020 Dec 17;533(4):1109-1114. PMID:33036753 doi:10.1016/j.bbrc.2020.09.124
↑ Snow AJD, Sharma M, Abayakoon P, Williams SJ, Blaza JN, Davies GJ. Structure and mechanism of sulfofructose transaldolase, a key enzyme in sulfoquinovose metabolism. Structure. 2023 Mar 2;31(3):244-252.e4. PMID:36805128 doi:10.1016/j.str.2023.01.010
↑ Snow AJD, Sharma M, Abayakoon P, Williams SJ, Blaza JN, Davies GJ. Structure and mechanism of sulfofructose transaldolase, a key enzyme in sulfoquinovose metabolism. Structure. 2023 Mar 2;31(3):244-252.e4. PMID:36805128 doi:10.1016/j.str.2023.01.010

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/8bc2"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8bc2 is ON HOLD
+==Ligand-Free Structure of the decameric sulfofructose transaldolase BmSF-TAL==
+<StructureSection load='8bc2' size='340' side='right'caption='[[8bc2]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<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]] 2.6&#8491;</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>
+== Function ==
+[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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8bc2" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Priestia aryabhattai]]
+[[Category: Blaza J]]
+[[Category: Davies GJ]]
+[[Category: Sharma M]]
+[[Category: Snow AJD]]

8bc2

From Proteopedia

Current revision

Ligand-Free Structure of the decameric sulfofructose transaldolase BmSF-TAL

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox