4phr
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4phr is ON HOLD Authors: Zhang, H., Wu, H. Description: Unknown function domain 1792 (DUF1792) with manganese) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Domain of unknown function 1792 (DUF1792) with manganese== | |
| + | <StructureSection load='4phr' size='340' side='right'caption='[[4phr]], [[Resolution|resolution]] 1.34Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4phr]] 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=4PHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PHR 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]] 1.34Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=4phr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4phr OCA], [https://pdbe.org/4phr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4phr RCSB], [https://www.ebi.ac.uk/pdbsum/4phr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4phr 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4phr" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptococcus parasanguinis FW213]] | ||
| + | [[Category: Wu H]] | ||
| + | [[Category: Zhang H]] | ||
Current revision
Domain of unknown function 1792 (DUF1792) with manganese
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