This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5i23

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:42, 27 May 2020

Crystal Structure of Agd31B, alpha-transglucosylase in Glycoside Hydrolase Family 31, in complex with Cyclophellitol Aziridine probe CF022

Structural highlights

5i23 is a 1 chain structure with sequence from Celju. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Gene:	agd31B, CJA_3248 (CELJU)
Activity:	Oligosaccharide 4-alpha-D-glucosyltransferase, with EC number 2.4.1.161
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/5i23"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Agd31B, alpha-transglucosylase in Glycoside Hydrolase Family 31, in complex with Cyclophellitol Aziridine probe CF022==
-<StructureSection load='5i23' size='340' side='right' caption='[[5i23]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
+<StructureSection load='5i23' size='340' side='right'caption='[[5i23]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5i23]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I23 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I23 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5i23]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Celju Celju]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I23 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5I23 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=66V:1-(8-{[(1S,2R,3S,4S,5R,6R)-2,3,4,5-TETRAHYDROXY-6-(HYDROXYMETHYL)CYCLOHEXYL]AMINO}OCTYL)TRIAZA-1,2-DIEN-2-IUM'>66V</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></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=66V:1-(8-{[(1S,2R,3S,4S,5R,6R)-2,3,4,5-TETRAHYDROXY-6-(HYDROXYMETHYL)CYCLOHEXYL]AMINO}OCTYL)TRIAZA-1,2-DIEN-2-IUM'>66V</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></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">agd31B, CJA_3248 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=498211 CELJU])</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='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=5i23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i23 OCA], [http://pdbe.org/5i23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i23 RCSB], [http://www.ebi.ac.uk/pdbsum/5i23 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i23 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=5i23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i23 OCA], [http://pdbe.org/5i23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i23 RCSB], [http://www.ebi.ac.uk/pdbsum/5i23 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i23 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 23: / Line 24: @@
 __TOC__
 </StructureSection>
+[[Category: Celju]]
+[[Category: Large Structures]]
 [[Category: Oligosaccharide 4-alpha-D-glucosyltransferase]]
 [[Category: Davies, G J]]

5i23

From Proteopedia

Revision as of 08:42, 27 May 2020

Crystal Structure of Agd31B, alpha-transglucosylase in Glycoside Hydrolase Family 31, in complex with Cyclophellitol Aziridine probe CF022

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox