View source for 2wq4


==N-terminal domain of BC2L-C Lectin from Burkholderia cenocepacia==
<StructureSection load='2wq4' size='340' side='right'caption='[[2wq4]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2wq4]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_J2315 Burkholderia cenocepacia J2315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WQ4 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]] 1.42&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SFU:METHYL+6-DEOXY-1-SELENO-ALPHA-L-GALACTOPYRANOSIDE'>SFU</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=2wq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wq4 OCA], [https://pdbe.org/2wq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wq4 RCSB], [https://www.ebi.ac.uk/pdbsum/2wq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wq4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B4EH86_BURCJ B4EH86_BURCJ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The opportunistic pathogen Burkholderia cenocepacia expresses several soluble lectins, among them BC2L-C. This lectin exhibits two domains: a C-terminal domain with high sequence similarity to the recently described calcium-dependent mannose-binding lectin BC2L-A, and an N-terminal domain of 156 amino acids without similarity to any known protein. The recombinant N-terminal BC2L-C domain is a new lectin with specificity for fucosylated human histo-blood group epitopes H-type 1, Lewis b, and Lewis Y, as determined by glycan array and isothermal titration calorimetry. Methylselenofucoside was used as ligand to solve the crystal structure of the N-terminal BC2L-C domain. Additional molecular modeling studies rationalized the preference for Lewis epitopes. The structure reveals a trimeric jellyroll arrangement with striking similarity to TNF-like proteins, and to BclA, the spore protein from Bacillus anthracis which may play an important role in bioadhesion of anthrax spores in human lungs.

A TNF-like trimeric lectin domain from Burkholderia cenocepacia with specificity for fucosylated human histo-blood group antigens.,Sulak O, Cioci G, Delia M, Lahmann M, Varrot A, Imberty A, Wimmerova M Structure. 2010 Jan 13;18(1):59-72. PMID:20152153<ref>PMID:20152153</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2wq4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Burkholderia cenocepacia J2315]]
[[Category: Large Structures]]
[[Category: Cioci G]]
[[Category: Delia M]]
[[Category: Imberty A]]
[[Category: Lahman M]]
[[Category: Sulak O]]
[[Category: Varrot A]]
[[Category: Wimmerova M]]