6uax

<table><tr><td colspan='2'>[[6uax]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Polyangium_cellulosum_(strain_so_ce56) Polyangium cellulosum (strain so ce56)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UAX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UAX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sce3275 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=448385 Polyangium cellulosum (strain So ce56)])</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=6uax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uax OCA], [http://pdbe.org/6uax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uax RCSB], [http://www.ebi.ac.uk/pdbsum/6uax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uax ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The fundamental and assorted roles of beta-1,3-glucans in nature are underpinned on diverse chemistry and molecular structures, demanding sophisticated and intricate enzymatic systems for their processing. In this work, the selectivity and modes of action of a glycoside hydrolase family active on beta-1,3-glucans were systematically investigated combining sequence similarity network, phylogeny, X-ray crystallography, enzyme kinetics, mutagenesis and molecular dynamics. This family exhibits a minimalist and versatile (alpha/beta)-barrel scaffold, which can harbor distinguishing exo or endo modes of action, including an ancillary-binding site for the anchoring of triple-helical beta-1,3-glucans. The substrate binding occurs via a hydrophobic knuckle complementary to the canonical curved conformation of beta-1,3-glucans or through a substrate conformational change imposed by the active-site topology of some fungal enzymes. Together, these findings expand our understanding of the enzymatic arsenal of bacteria and fungi for the breakdown and modification of beta-1,3-glucans, which can be exploited for biotechnological applications.

 

== References ==

[[Category: Costa, P A.C R]]

[[Category: Domingues, M N]]

[[Category: Lima, E A]]

[[Category: Mandelli, F]]

[[Category: Murakami, M T]]

[[Category: Santos, C R]]

[[Category: Vieira, P S]]

[[Category: Hydrolase]]