5man: Difference between revisions

Latest revision as of 18:35, 1 November 2023

Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose

Structural highlights

5man is a 1 chain structure with sequence from Bifidobacterium adolescentis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.04Å
Ligands:	GLC, PRD_900052
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SUCP_BIFAA Catalyzes the reversible phosphorolysis of sucrose into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose (PubMed:14740189, PubMed:20691225). Is involved in sucrose degradation. Also displays transglucosylation activity in vitro, by transferring the glucosyl moiety of Glc1P to a broad range of monomeric sugars, such as D- and L-arabinose, D- and L-arabitol, and xylitol (PubMed:14740189).^[1] ^[2]

Publication Abstract from PubMed

Here we present a point mutation-triggered domain shift which switches the acceptor preference of a sucrose phosphorylase from phosphate to a variety of large polyphenolic compounds including resveratrol and quercetin, enabling their efficient glucosylation. The variant possesses a high affinity for aromatic substrates due to newly introduced pi-pi- and hydrophobic interactions in the altered active site. The domain shift brings about a substantially enlarged and multifunctional active site for polyphenol glucosylation and rare disaccharide production. The crystal structure of the variant with its product resveratrol-3-alpha-d-glucoside allows the prediction of the substrate scope and regioselectivity of the aromatic compounds' glucosylation sites.

Switching enzyme specificity from phosphate to resveratrol glucosylation.,Kraus M, Grimm C, Seibel J Chem Commun (Camb). 2017 Nov 9;53(90):12181-12184. doi: 10.1039/c7cc05993k. PMID:29057405^[3]

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

References

↑ van den Broek LA, van Boxtel EL, Kievit RP, Verhoef R, Beldman G, Voragen AG. Physico-chemical and transglucosylation properties of recombinant sucrose phosphorylase from Bifidobacterium adolescentis DSM20083. Appl Microbiol Biotechnol. 2004 Aug;65(2):219-27. Epub 2004 Jan 22. PMID:14740189 doi:https://dx.doi.org/10.1007/s00253-003-1534-x
↑ Cerdobbel A, Desmet T, De Winter K, Maertens J, Soetaert W. Increasing the thermostability of sucrose phosphorylase by multipoint covalent immobilization. J Biotechnol. 2010 Oct 1;150(1):125-30. doi: 10.1016/j.jbiotec.2010.07.029. Epub , 2010 Aug 4. PMID:20691225 doi:https://dx.doi.org/10.1016/j.jbiotec.2010.07.029
↑ Kraus M, Grimm C, Seibel J. Switching enzyme specificity from phosphate to resveratrol glucosylation. Chem Commun (Camb). 2017 Nov 9;53(90):12181-12184. doi: 10.1039/c7cc05993k. PMID:29057405 doi:https://dx.doi.org/10.1039/c7cc05993k

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] van den Broek LA, van Boxtel EL, Kievit RP, Verhoef R, Beldman G, Voragen AG. Physico-chemical and transglucosylation properties of recombinant sucrose phosphorylase from Bifidobacterium adolescentis DSM20083. Appl Microbiol Biotechnol. 2004 Aug;65(2):219-27. Epub 2004 Jan 22. PMID:14740189 doi:https://dx.doi.org/10.1007/s00253-003-1534-x

[2] Cerdobbel A, Desmet T, De Winter K, Maertens J, Soetaert W. Increasing the thermostability of sucrose phosphorylase by multipoint covalent immobilization. J Biotechnol. 2010 Oct 1;150(1):125-30. doi: 10.1016/j.jbiotec.2010.07.029. Epub , 2010 Aug 4. PMID:20691225 doi:https://dx.doi.org/10.1016/j.jbiotec.2010.07.029

[3] Kraus M, Grimm C, Seibel J. Switching enzyme specificity from phosphate to resveratrol glucosylation. Chem Commun (Camb). 2017 Nov 9;53(90):12181-12184. doi: 10.1039/c7cc05993k. PMID:29057405 doi:https://dx.doi.org/10.1039/c7cc05993k

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='5man' size='340' side='right'caption='[[5man]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5man]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_1.2190 As 1.2190]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5MAN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5man]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_adolescentis Bifidobacterium adolescentis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MAN FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sucP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1680 AS 1.2190])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900052:alpha-nigerose'>PRD_900052</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.7 2.4.1.7] </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=5man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5man OCA], [https://pdbe.org/5man PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5man RCSB], [https://www.ebi.ac.uk/pdbsum/5man PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5man 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=5man FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5man OCA], [http://pdbe.org/5man PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5man RCSB], [http://www.ebi.ac.uk/pdbsum/5man PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5man ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/SUCP_BIFAA SUCP_BIFAA] Catalyzes the reversible phosphorolysis of sucrose into alpha-D-glucose 1-phosphate (Glc1P) and D-fructose (PubMed:14740189, PubMed:20691225). Is involved in sucrose degradation. Also displays transglucosylation activity in vitro, by transferring the glucosyl moiety of Glc1P to a broad range of monomeric sugars, such as D- and L-arabinose, D- and L-arabitol, and xylitol (PubMed:14740189).<ref>PMID:14740189</ref> <ref>PMID:20691225</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: As 1 2190]]
+[[Category: Bifidobacterium adolescentis]]
 [[Category: Large Structures]]
-[[Category: Transferase]]
+[[Category: Grimm C]]
-[[Category: Grimm, C]]
+[[Category: Kraus M]]
-[[Category: Kraus, M]]
-[[Category: Enzyme design]]
-[[Category: Resveratrol]]
-[[Category: Sucrose phosphorylase]]

5man: Difference between revisions

Latest revision as of 18:35, 1 November 2023

Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose

Structural highlights

Function

Publication Abstract from PubMed

References

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