7ne2: Difference between revisions
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The | ==Crystal structure of class I SFP aldolase YihT from Salmonella enterica with SFP/ DHAP (Schiff base complex with active site Lys193)== | ||
<StructureSection load='7ne2' size='340' side='right'caption='[[7ne2]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7ne2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NE2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=U8W:(2~{S},3~{S},4~{R})-2,3,4,5-tetrakis(oxidanyl)-6-phosphonooxy-hexane-1-sulfonic+acid'>U8W</scene>, <scene name='pdbligand=U8Z:[(~{E})-2,3-bis(oxidanyl)prop-1-enyl]+dihydrogen+phosphate'>U8Z</scene></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=7ne2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ne2 OCA], [https://pdbe.org/7ne2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ne2 RCSB], [https://www.ebi.ac.uk/pdbsum/7ne2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ne2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SQUT_SALTY SQUT_SALTY] Cleaves 6-deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA).[HAMAP-Rule:MF_01912] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The sulfosugar sulfoquinovose (SQ) is produced by essentially all photosynthetic organisms on Earth and is metabolized by bacteria through the process of sulfoglycolysis. The sulfoglycolytic Embden-Meyerhof-Parnas pathway metabolizes SQ to produce dihydroxyacetone phosphate and sulfolactaldehyde and is analogous to the classical Embden-Meyerhof-Parnas glycolysis pathway for the metabolism of glucose-6-phosphate, though the former only provides one C3 fragment to central metabolism, with excretion of the other C3 fragment as dihydroxypropanesulfonate. Here, we report a comprehensive structural and biochemical analysis of the three core steps of sulfoglycolysis catalyzed by SQ isomerase, sulfofructose (SF) kinase, and sulfofructose-1-phosphate (SFP) aldolase. Our data show that despite the superficial similarity of this pathway to glycolysis, the sulfoglycolytic enzymes are specific for SQ metabolites and are not catalytically active on related metabolites from glycolytic pathways. This observation is rationalized by three-dimensional structures of each enzyme, which reveal the presence of conserved sulfonate binding pockets. We show that SQ isomerase acts preferentially on the beta-anomer of SQ and reversibly produces both SF and sulforhamnose (SR), a previously unknown sugar that acts as a derepressor for the transcriptional repressor CsqR that regulates SQ-utilization. We also demonstrate that SF kinase is a key regulatory enzyme for the pathway that experiences complex modulation by the metabolites SQ, SLA, AMP, ADP, ATP, F6P, FBP, PEP, DHAP, and citrate, and we show that SFP aldolase reversibly synthesizes SFP. This body of work provides fresh insights into the mechanism, specificity, and regulation of sulfoglycolysis and has important implications for understanding how this biochemistry interfaces with central metabolism in prokaryotes to process this major repository of biogeochemical sulfur. | |||
Molecular Basis of Sulfosugar Selectivity in Sulfoglycolysis.,Sharma M, Abayakoon P, Epa R, Jin Y, Lingford JP, Shimada T, Nakano M, Mui JW, Ishihama A, Goddard-Borger ED, Davies GJ, Williams SJ ACS Cent Sci. 2021 Mar 24;7(3):476-487. doi: 10.1021/acscentsci.0c01285. Epub, 2021 Feb 23. PMID:33791429<ref>PMID:33791429</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7ne2" style="background-color:#fffaf0;"></div> | ||
[[Category: Davies | |||
==See Also== | |||
*[[Aldolase 3D structures|Aldolase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Salmonella enterica]] | |||
[[Category: Davies GJ]] | |||
[[Category: Sharma M]] | |||
Latest revision as of 15:33, 1 February 2024
Crystal structure of class I SFP aldolase YihT from Salmonella enterica with SFP/ DHAP (Schiff base complex with active site Lys193)Crystal structure of class I SFP aldolase YihT from Salmonella enterica with SFP/ DHAP (Schiff base complex with active site Lys193)
Structural highlights
FunctionSQUT_SALTY Cleaves 6-deoxy-6-sulfo-D-fructose 1-phosphate (SFP) to form dihydroxyacetone phosphate (DHAP) and 3-sulfolactaldehyde (SLA).[HAMAP-Rule:MF_01912] Publication Abstract from PubMedThe sulfosugar sulfoquinovose (SQ) is produced by essentially all photosynthetic organisms on Earth and is metabolized by bacteria through the process of sulfoglycolysis. The sulfoglycolytic Embden-Meyerhof-Parnas pathway metabolizes SQ to produce dihydroxyacetone phosphate and sulfolactaldehyde and is analogous to the classical Embden-Meyerhof-Parnas glycolysis pathway for the metabolism of glucose-6-phosphate, though the former only provides one C3 fragment to central metabolism, with excretion of the other C3 fragment as dihydroxypropanesulfonate. Here, we report a comprehensive structural and biochemical analysis of the three core steps of sulfoglycolysis catalyzed by SQ isomerase, sulfofructose (SF) kinase, and sulfofructose-1-phosphate (SFP) aldolase. Our data show that despite the superficial similarity of this pathway to glycolysis, the sulfoglycolytic enzymes are specific for SQ metabolites and are not catalytically active on related metabolites from glycolytic pathways. This observation is rationalized by three-dimensional structures of each enzyme, which reveal the presence of conserved sulfonate binding pockets. We show that SQ isomerase acts preferentially on the beta-anomer of SQ and reversibly produces both SF and sulforhamnose (SR), a previously unknown sugar that acts as a derepressor for the transcriptional repressor CsqR that regulates SQ-utilization. We also demonstrate that SF kinase is a key regulatory enzyme for the pathway that experiences complex modulation by the metabolites SQ, SLA, AMP, ADP, ATP, F6P, FBP, PEP, DHAP, and citrate, and we show that SFP aldolase reversibly synthesizes SFP. This body of work provides fresh insights into the mechanism, specificity, and regulation of sulfoglycolysis and has important implications for understanding how this biochemistry interfaces with central metabolism in prokaryotes to process this major repository of biogeochemical sulfur. Molecular Basis of Sulfosugar Selectivity in Sulfoglycolysis.,Sharma M, Abayakoon P, Epa R, Jin Y, Lingford JP, Shimada T, Nakano M, Mui JW, Ishihama A, Goddard-Borger ED, Davies GJ, Williams SJ ACS Cent Sci. 2021 Mar 24;7(3):476-487. doi: 10.1021/acscentsci.0c01285. Epub, 2021 Feb 23. PMID:33791429[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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