View source for 4peu


==Structure of the polysaccharide lyase-like protein Cthe_2159 from C. thermocellum, native form with Calcium bound==
<StructureSection load='4peu' size='340' side='right'caption='[[4peu]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4peu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus_ATCC_27405 Acetivibrio thermocellus ATCC 27405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PEU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PEU 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]] 1.8001&#8491;</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></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=4peu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4peu OCA], [https://pdbe.org/4peu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4peu RCSB], [https://www.ebi.ac.uk/pdbsum/4peu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4peu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CBDP_ACET2 CBDP_ACET2] Binds cellulosic and pectic substrates. Displays no enzyme activity (in vitro).<ref>PMID:25286843</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Microorganisms that degrade biomass produce diverse assortments of carbohydrate-active enzymes and binding modules. Despite tremendous advances in the genomic sequencing of these organisms, many genes do not have an ascribed function owing to low sequence identity to genes that have been annotated. Consequently, biochemical and structural characterization of genes with unknown function is required to complement the rapidly growing pool of genomic sequencing data. A protein with previously unknown function (Cthe_2159) was recently isolated in a genome-wide screen using phage display to identify cellulose-binding protein domains from the biomass-degrading bacterium Clostridium thermocellum. Here, the crystal structure of Cthe_2159 is presented and it is shown that it is a unique right-handed parallel beta-helix protein. Despite very low sequence identity to known beta-helix or carbohydrate-active proteins, Cthe_2159 displays structural features that are very similar to those of polysaccharide lyase (PL) families 1, 3, 6 and 9. Cthe_2159 is conserved across bacteria and some archaea and is a member of the domain of unknown function family DUF4353. This suggests that Cthe_2159 is the first representative of a previously unknown family of cellulose and/or acid-sugar binding beta-helix proteins that share structural similarities with PLs. Importantly, these results demonstrate how functional annotation by biochemical and structural analysis remains a critical tool in the characterization of new gene products.

A new family of beta-helix proteins with similarities to the polysaccharide lyases.,Close DW, D'Angelo S, Bradbury AR Acta Crystallogr D Biol Crystallogr. 2014 Oct 1;70(Pt 10):2583-92. doi:, 10.1107/S1399004714015934. Epub 2014 Sep 27. PMID:25286843<ref>PMID:25286843</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4peu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acetivibrio thermocellus ATCC 27405]]
[[Category: Large Structures]]
[[Category: Bradbury ARM]]
[[Category: Close DW]]
[[Category: D'Angelo S]]