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5i24

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Current revision

Crystal Structure of Agd31B, alpha-transglucosylase in Glycoside Hydrolase Family 31, in complex with Cyclophellitol Aziridine probe CF021

Structural highlights

5i24 is a 1 chain structure with sequence from Cellvibrio japonicus Ueda107. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OL4AG_CELJU Alpha-transglucosylase that specifically transfers single glucosyl units from alpha(1->4)-glucans to the non-reducing terminal 4-OH of glucose and alpha(1->4)- and alpha(1->6)-linked glucosyl residues. Acts on amylose, amylopectin, glycogen and maltooligosaccharides, with the highest activity with maltotriose as a donor, and also accepts maltose. Does not act as a hydrolase: weak hydrolysis activity is only observed on the disaccharide maltose.^[1]

Publication Abstract from PubMed

The development of small molecule activity-based probes (ABPs) is an evolving and powerful area of chemistry. There is a major need for synthetically accessible and specific ABPs to advance our understanding of enzymes in health and disease. alpha-Glucosidases are involved in diverse physiological processes including carbohydrate assimilation in the gastrointestinal tract, glycoprotein processing in the endoplasmic reticulum (ER), and intralysosomal glycogen catabolism. Inherited deficiency of the lysosomal acid alpha-glucosidase (GAA) causes the lysosomal glycogen storage disorder, Pompe disease. Here, we design a synthetic route for fluorescent and biotin-modified ABPs for in vitro and in situ monitoring of alpha-glucosidases. We show, through mass spectrometry, gel electrophoresis, and X-ray crystallography, that alpha-glucopyranose configured cyclophellitol aziridines label distinct retaining alpha-glucosidases including GAA and ER alpha-glucosidase II, and that this labeling can be tuned by pH. We illustrate a direct diagnostic application in Pompe disease patient cells, and discuss how the probes may be further exploited for diverse applications.

Detection of Active Mammalian GH31 alpha-Glucosidases in Health and Disease Using In-Class, Broad-Spectrum Activity-Based Probes.,Jiang J, Kuo CL, Wu L, Franke C, Kallemeijn WW, Florea BI, van Meel E, van der Marel GA, Codee JD, Boot RG, Davies GJ, Overkleeft HS, Aerts JM ACS Cent Sci. 2016 May 25;2(5):351-8. doi: 10.1021/acscentsci.6b00057. Epub 2016 , Apr 26. PMID:27280170^[2]

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

References

↑ Larsbrink J, Izumi A, Hemsworth GR, Davies GJ, Brumer H. Structural enzymology of Cellvibrio japonicus Agd31B reveals alpha-transglucosylase activity in glycoside hydrolase family 31. J Biol Chem. 2012 Nov 6. PMID:23132856 doi:http://dx.doi.org/10.1074/jbc.M112.416511
↑ Jiang J, Kuo CL, Wu L, Franke C, Kallemeijn WW, Florea BI, van Meel E, van der Marel GA, Codee JD, Boot RG, Davies GJ, Overkleeft HS, Aerts JM. Detection of Active Mammalian GH31 alpha-Glucosidases in Health and Disease Using In-Class, Broad-Spectrum Activity-Based Probes. ACS Cent Sci. 2016 May 25;2(5):351-8. doi: 10.1021/acscentsci.6b00057. Epub 2016 , Apr 26. PMID:27280170 doi:http://dx.doi.org/10.1021/acscentsci.6b00057

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/5i24"

Categories: Cellvibrio japonicus Ueda107 | Large Structures | Davies GJ | Wu L

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Agd31B, alpha-transglucosylase in Glycoside Hydrolase Family 31, in complex with Cyclophellitol Aziridine probe CF021==
-<StructureSection load='5i24' size='340' side='right' caption='[[5i24]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+<StructureSection load='5i24' size='340' side='right'caption='[[5i24]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5i24]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I24 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I24 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5i24]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus_Ueda107 Cellvibrio japonicus Ueda107]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I24 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I24 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=66U:(1R,2S,3S,4R,5S,6R)-5-AMINO-6-(HYDROXYMETHYL)CYCLOHEXANE-1,2,3,4-TETROL'>66U</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.85&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oligosaccharide_4-alpha-D-glucosyltransferase Oligosaccharide 4-alpha-D-glucosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.161 2.4.1.161] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=66U:(1R,2S,3S,4R,5S,6R)-5-AMINO-6-(HYDROXYMETHYL)CYCLOHEXANE-1,2,3,4-TETROL'>66U</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=5i24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i24 OCA], [http://pdbe.org/5i24 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i24 RCSB], [http://www.ebi.ac.uk/pdbsum/5i24 PDBsum]</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=5i24 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i24 OCA], [https://pdbe.org/5i24 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i24 RCSB], [https://www.ebi.ac.uk/pdbsum/5i24 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i24 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/OL4AG_CELJU OL4AG_CELJU]] Alpha-transglucosylase that specifically transfers single glucosyl units from alpha(1->4)-glucans to the non-reducing terminal 4-OH of glucose and alpha(1->4)- and alpha(1->6)-linked glucosyl residues. Acts on amylose, amylopectin, glycogen and maltooligosaccharides, with the highest activity with maltotriose as a donor, and also accepts maltose. Does not act as a hydrolase: weak hydrolysis activity is only observed on the disaccharide maltose.<ref>PMID:23132856</ref>
+[https://www.uniprot.org/uniprot/OL4AG_CELJU OL4AG_CELJU] Alpha-transglucosylase that specifically transfers single glucosyl units from alpha(1->4)-glucans to the non-reducing terminal 4-OH of glucose and alpha(1->4)- and alpha(1->6)-linked glucosyl residues. Acts on amylose, amylopectin, glycogen and maltooligosaccharides, with the highest activity with maltotriose as a donor, and also accepts maltose. Does not act as a hydrolase: weak hydrolysis activity is only observed on the disaccharide maltose.<ref>PMID:23132856</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Oligosaccharide 4-alpha-D-glucosyltransferase]]
+[[Category: Cellvibrio japonicus Ueda107]]
-[[Category: Davies, G J]]
+[[Category: Large Structures]]
-[[Category: Wu, L]]
+[[Category: Davies GJ]]
-[[Category: Alpha glycosidase]]
+[[Category: Wu L]]
-[[Category: Cyclophellitol aziridine]]
-[[Category: Hydrolase]]
-[[Category: Inhibitor]]
-[[Category: Probe]]

5i24

From Proteopedia

Current revision

Crystal Structure of Agd31B, alpha-transglucosylase in Glycoside Hydrolase Family 31, in complex with Cyclophellitol Aziridine probe CF021

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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