View source for 4ozo


==Crystal structure of an a-L-fucosidase GH29 from Bacteroides thetaiotaomicron (BT2192) in complex with oNPTG==
<StructureSection load='4ozo' size='340' side='right'caption='[[4ozo]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ozo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OZO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OZO 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OTN:(2R,3R,4S,5R,6S)-2-(HYDROXYMETHYL)-6-(2-NITROPHENYL)SULFANYL-OXANE-3,4,5-TRIOL'>OTN</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=4ozo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ozo OCA], [https://pdbe.org/4ozo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ozo RCSB], [https://www.ebi.ac.uk/pdbsum/4ozo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ozo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8A5P6_BACTN Q8A5P6_BACTN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycosyl hydrolase (GH) family 29 (CAZy database) consists of retaining alpha-l-fucosidases. We have identified BT2192, a protein from Bacteroides thetaiotaomicron, as the first GH29 representative exhibiting both weak alpha-l-fucosidase and beta-d-galactosidase activities. Determination and analysis of X-ray structures of BT2192 in complex with beta-d-galactoside competitive inhibitors showed a new binding mode different from that of known GH29 enzymes. Three point mutations, specific to BT2192, prevent the canonical GH29 substrate alpha-l-fucose from binding efficiently to the fucosidase-like active site relative to other GH29 enzymes. beta-d-Galactoside analogues bind and interact in a second pocket, which is not visible in other reported GH29 structures. Molecular simulations helped in the assessment of the flexibility of both substrates in their respective pocket. Hydrolysis of the fucosyl moiety from the putative natural substrates like 3-fucosyllactose or LewisX antigen would be mainly due to the efficient interactions with the galactosyl moiety, in the second binding site, located more than 6-7 A apart.

Unraveling the Substrate Recognition Mechanism and Specificity of the Unusual Glycosyl Hydrolase Family 29 BT2192 from Bacteroides thetaiotaomicron.,Guillotin L, Lafite P, Daniellou R Biochemistry. 2014 Feb 27. PMID:24527659<ref>PMID:24527659</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ozo" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacteroides thetaiotaomicron VPI-5482]]
[[Category: Large Structures]]
[[Category: Daniellou R]]
[[Category: Guillotin L]]
[[Category: Lafite P]]