5hec: Difference between revisions

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'''Unreleased structure'''


The entry 5hec is ON HOLD  until Paper Publication
==CgT structure in dimer==
<StructureSection load='5hec' size='340' side='right' caption='[[5hec]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5hec]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HEC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HEC FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hea|5hea]]</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=5hec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hec OCA], [http://pdbe.org/5hec PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hec RCSB], [http://www.ebi.ac.uk/pdbsum/5hec PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hec ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Serine-rich repeat glycoproteins (SRRPs) conserved in streptococci and staphylococci are important for bacterial colonization and pathogenesis. Fap1, a well-studied SRRP is a major surface constituent of Streptococcus parasanguinis and is required for bacterial adhesion and biofilm formation. Biogenesis of Fap1 is a multi-step process that involves both glycosylation and secretion. A series of glycosyltransferases catalyze sequential glycosylation of Fap1. We have identified a unique hybrid protein dGT1(dual glycosyltransferase 1) that contains two distinct domains. N-terminal DUF1792 is a novel GT-D type glycosyltransferase, transferring Glc residues to Glc-GlcNAc-modified Fap1. C-terminal dGT1 (CgT) is predicted to possess a typical GT-A type glycosyltransferase, however the activity remains unknown. In this study, we determine that CgT is a distinct glycosyltransferase, transferring GlcNAc residues to Glc-Glc-GlcNAc-modified Fap1. 2.4 A X-ray crystal structure reveals that CgT has a unique binding domain consisting of three alpha helices in addition to a typical GT-A type glycosyltransferase domain. The helical domain is crucial for the oligomerization of CgT. Structural and biochemical studies revealed that the helix domain is required for the protein-protein interaction and crucial for the glycosyltransferase activity of CgT in vitro and in vivo. As the helix domain presents a novel structural fold, we conclude that CgT represents a new member of GT-A type glycosyltransferases.


Authors: Zhang, H., Wu, H.
A New Helical Binding Domain Mediates a Unique Glycosyltransferase Activity of a Bifunctional Protein.,Zhang H, Zhou M, Yang T, Haslam SM, Dell A, Wu H J Biol Chem. 2016 Aug 17. pii: jbc.M116.731695. PMID:27539847<ref>PMID:27539847</ref>


Description: CgT structure in dimer
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5hec" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Wu, H]]
[[Category: Zhang, H]]
[[Category: Zhang, H]]
[[Category: Wu, H]]
[[Category: Glycosyltransferase]]
[[Category: Helix binding domain]]
[[Category: Transferase]]
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