View source for 4phs


==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 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=4PHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PHS 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]] 1.54&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</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=4phs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4phs OCA], [https://pdbe.org/4phs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4phs RCSB], [https://www.ebi.ac.uk/pdbsum/4phs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4phs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I1ZPA1_STRPA I1ZPA1_STRPA] 
<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 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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4phs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus parasanguinis FW213]]
[[Category: Wu H]]
[[Category: Zhang H]]