3q3e

<StructureSection load='3q3e' size='340' side='right' caption='[[3q3e]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[3q3e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Actinobacillus_pleuropneumoniae_4074 Actinobacillus pleuropneumoniae 4074]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q3E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q3E FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3q3h|3q3h]], [[3q3i|3q3i]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APL_1635, appser1_17560 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=228399 Actinobacillus pleuropneumoniae 4074])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3q3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q3e OCA], [http://pdbe.org/3q3e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q3e RCSB], [http://www.ebi.ac.uk/pdbsum/3q3e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q3e ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Glycosylation of proteins is a fundamental process that influences protein function. The Haemophilus influenzae HMW1 adhesin is an N-linked glycoprotein that mediates adherence to respiratory epithelium, an essential early step in the pathogenesis of H. influenzae disease. HMW1 is glycosylated by HMW1C, a novel glycosyltransferase in the GT41 family that creates N-glycosidic linkages with glucose and galactose at asparagine residues and di-glucose linkages at sites of glucose modification. Here we report the crystal structure of Actinobacillus pleuropneumoniae HMW1C (ApHMW1C), a functional homolog of HMW1C. The structure of ApHMW1C contains an N-terminal all alpha-domain (AAD) fold and a C-terminal GT-B fold with two Rossmann-like domains and lacks the tetratricopeptide repeat fold characteristic of human GlcNAc transferase and other members of the GT41 family. The GT-B fold harbors the binding site for UDP-hexose, and the interface of the AAD fold and the GT-B fold forms a unique groove with potential to accommodate the acceptor protein. Structure-based functional analyses demonstrated that the HMW1C protein shares the same structure as ApHMW1C and provided insights into the unique bi-functional activity of HMW1C and ApHMW1C, suggesting an explanation for the similarities and differences of the HMW1C-like proteins compared to other GT41 family members.

Structural insights into the glycosyltransferase activity of the Actinobacillus pleuropneumoniae HMW1C-like protein.,Kawai F, Grass S, Kim Y, Choi KJ, St Geme JW, Yeo HJ J Biol Chem. 2011 Sep 9. PMID:21908603<ref>PMID:21908603</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 3q3e" style="background-color:#fffaf0;"></div>

*[[Glycosyltransferase|Glycosyltransferase]]

[[Category: Actinobacillus pleuropneumoniae 4074]]

[[Category: Kawai, F]]

[[Category: Yeo, H J]]

[[Category: Hmw1]]

[[Category: Transferase]]