View source for 5flw


==Crystal structure of putative exo-beta-1,3-galactanase from Bifidobacterium bifidum s17==
<StructureSection load='5flw' size='340' side='right'caption='[[5flw]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5flw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_bifidum_S17 Bifidobacterium bifidum S17]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FLW 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]] 1.401&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</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=5flw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5flw OCA], [https://pdbe.org/5flw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5flw RCSB], [https://www.ebi.ac.uk/pdbsum/5flw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5flw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E4VCC5_BIFBI E4VCC5_BIFBI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Given the current interest in second-generation biofuels, carbohydrate-active enzymes have become the most important tool to overcome the structural recalcitrance of the plant cell wall. While some glycoside hydrolase families have been exhaustively described, others remain poorly characterized, especially with regard to structural information. The family 43 glycoside hydrolases are a diverse group of inverting enzymes; the available structure information on these enzymes is mainly from xylosidases and arabinofuranosidase. Currently, only one structure of an exo-beta-1,3-galactanase is available. Here, the production, crystallization and structure determination of a putative exo-beta-1,3-galactanase from Bifidobacterium bifidum S17 (BbGal43A) are described. BbGal43A was successfully produced and showed activity towards synthetic galactosides. BbGal43A was subsequently crystallized and data were collected to 1.4 A resolution. The structure shows a single-domain molecule, differing from known homologues, and crystal contact analysis predicts the formation of a dimer in solution. Further biochemical studies are necessary to elucidate the differences between BbGal43A and its characterized homologues.

Crystal structure of a putative exo-beta-1,3-galactanase from Bifidobacterium bifidum S17.,Godoy AS, de Lima MZ, Camilo CM, Polikarpov I Acta Crystallogr F Struct Biol Commun. 2016 Apr;72(Pt 4):288-93. doi:, 10.1107/S2053230X16003617. Epub 2016 Mar 16. PMID:27050262<ref>PMID:27050262</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5flw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bifidobacterium bifidum S17]]
[[Category: Large Structures]]
[[Category: Camilo CM]]
[[Category: Godoy AS]]
[[Category: Muniz JRC]]
[[Category: Polikarpov I]]
[[Category: Ramia MP]]
[[Category: De Lima MZT]]