5man

From Proteopedia

(Difference between revisions)

Current revision

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:	,
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:http://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:http://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:http://dx.doi.org/10.1039/c7cc05993k

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/5man"

Categories: Bifidobacterium adolescentis | Large Structures | Grimm C | Kraus M

@@ Line 1: / Line 1: @@
 ==Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose==
-<StructureSection load='5man' size='340' side='right' caption='[[5man]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
+<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. 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://oca.weizmann.ac.il/oca-docs/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"><scene name='pdbligand=NGR:3-O-ALPHA-D-GLUCOPYRANOSYL-ALPHA-D-GLUCOPYRANOSE'>NGR</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='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='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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/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>
+<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>
 </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 21: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Transferase]]
+[[Category: Bifidobacterium adolescentis]]
-[[Category: Grimm, C]]
+[[Category: Large Structures]]
-[[Category: Kraus, M]]
+[[Category: Grimm C]]
-[[Category: Enzyme design]]
+[[Category: Kraus M]]
-[[Category: Resveratrol]]
-[[Category: Sucrose phosphorylase]]

5man

From Proteopedia

Current revision

Structure of sucrose phosphorylase from Bifidobacterium adolescentis bound to nigerose

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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