4phs: Difference between revisions

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'''Unreleased structure'''
==Selenomethionine substituted structure of domain of unknown function 1792 (DUF1792)==
<StructureSection load='4phs' size='340' side='right' caption='[[4phs]], [[Resolution|resolution]] 1.54&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4phs]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PHS FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene><br>
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pfx|4pfx]], [[4phr|4phr]]</td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4phs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4phs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4phs RCSB], [http://www.ebi.ac.uk/pdbsum/4phs PDBsum]</span></td></tr>
<table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
More than 33,000 glycosyltransferases have been identified. Structural studies, however, have only revealed two distinct glycosyltransferase (GT) folds, GT-A and GT-B. Here we report a 1.34-A resolution X-ray crystallographic structure of a previously uncharacterized 'domain of unknown function' 1792 (DUF1792) and show that the domain adopts a new fold and is required for glycosylation of a family of serine-rich repeat streptococcal adhesins. Biochemical studies reveal that the domain is a glucosyltransferase, and it catalyses the transfer of glucose to the branch point of the hexasaccharide O-linked to the serine-rich repeat of the bacterial adhesin, Fap1 of Streptococcus parasanguinis. DUF1792 homologues from both Gram-positive and Gram-negative bacteria also exhibit the activity. Thus, DUF1792 represents a new family of glycosyltransferases; therefore, we designate it as a GT-D glycosyltransferase fold. As the domain is highly conserved in bacteria and not found in eukaryotes, it can be explored as a new antibacterial target.


The entry 4phs is ON HOLD
The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold.,Zhang H, Zhu F, Yang T, Ding L, Zhou M, Li J, Haslam SM, Dell A, Erlandsen H, Wu H Nat Commun. 2014 Jul 15;5:4339. doi: 10.1038/ncomms5339. PMID:25023666<ref>PMID:25023666</ref>


Authors: Zhang, H., Wu, H.
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
Description: Selenomethionyl substituted unknown function domain 1792 (DUF1792)
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Wu, H.]]
[[Category: Zhang, H.]]
[[Category: And duf1792]]
[[Category: Glycosyltransferase]]
[[Category: Streptococcal adhesin]]
[[Category: Transferase]]