View source for 2yfn


==galactosidase domain of alpha-galactosidase-sucrose kinase, AgaSK==
<StructureSection load='2yfn' size='340' side='right'caption='[[2yfn]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2yfn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ruminococcus_gnavus_E1 Ruminococcus gnavus E1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YFN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YFN 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]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=2yfn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yfn OCA], [https://pdbe.org/2yfn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yfn RCSB], [https://www.ebi.ac.uk/pdbsum/2yfn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yfn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AGASK_RUMGN AGASK_RUMGN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
alpha-Galactosides are non-digestible carbohydrates widely distributed in plants. They are a potential source of energy in our daily food, and their assimilation by microbiota may play a role in obesity. In the intestinal tract, they are degraded by microbial glycosidases, which are often modular enzymes with catalytic domains linked to carbohydrate-binding modules. Here we introduce a bifunctional enzyme from the human intestinal bacterium Ruminococcus gnavus E1, alpha-galactosidase/sucrose kinase (AgaSK). Sequence analysis showed that AgaSK is composed of two domains: one closely related to alpha-galactosidases from glycoside hydrolase family GH36 and the other containing a nucleotide-binding motif. Its biochemical characterization showed that AgaSK is able to hydrolyze melibiose and raffinose to galactose and either glucose or sucrose, respectively, and to specifically phosphorylate sucrose on the C6 position of glucose in the presence of ATP. The production of sucrose-6-P directly from raffinose points toward a glycolytic pathway in bacteria, not described so far. The crystal structures of the galactosidase domain in the apo form and in complex with the product shed light onto the reaction and substrate recognition mechanisms and highlight an oligomeric state necessary for efficient substrate binding and suggesting a cross-talk between the galactose and kinase domains.

alpha-Galactosidase/Sucrose Kinase (AgaSK), a Novel Bifunctional Enzyme from the Human Microbiome Coupling Galactosidase and Kinase Activities.,Bruel L, Sulzenbacher G, Cervera Tison M, Pujol A, Nicoletti C, Perrier J, Galinier A, Ropartz D, Fons M, Pompeo F, Giardina T J Biol Chem. 2011 Nov 25;286(47):40814-23. Epub 2011 Sep 19. PMID:21931163<ref>PMID:21931163</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2yfn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Bruel L]]
[[Category: Fons M]]
[[Category: Galinier A]]
[[Category: Giardina T]]
[[Category: Nicoletti C]]
[[Category: Perrier J]]
[[Category: Pompeo F]]
[[Category: Pujol A]]
[[Category: Ropartz D]]
[[Category: Sulzenbacher G]]
[[Category: Tison-Cervera M]]