5hec: Difference between revisions
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New page: '''Unreleased structure''' The entry 5hec is ON HOLD Authors: Zhang, H., Wu, H. Description: CgT structure in dimer Category: Unreleased Structures Category: Zhang, H [[Categor... |
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The | ==CgT structure in dimer== | ||
<StructureSection load='5hec' size='340' side='right'caption='[[5hec]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hec]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_parasanguinis_FW213 Streptococcus parasanguinis FW213]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5HEC 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]] 2.395Å</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=5hec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hec OCA], [https://pdbe.org/5hec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hec RCSB], [https://www.ebi.ac.uk/pdbsum/5hec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hec ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/I1ZPA1_STRPA I1ZPA1_STRPA] | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5hec" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus parasanguinis FW213]] | |||
[[Category: Wu H]] | |||
[[Category: Zhang H]] | |||
