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| | <StructureSection load='4phr' size='340' side='right'caption='[[4phr]], [[Resolution|resolution]] 1.34Å' scene=''> | | <StructureSection load='4phr' size='340' side='right'caption='[[4phr]], [[Resolution|resolution]] 1.34Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4phr]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PHR FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pfx|4pfx]], [[4phs|4phs]]</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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">galT1, Spaf_1933 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1114965 Streptococcus parasanguinis FW213])</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=4phr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4phr OCA], [http://pdbe.org/4phr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4phr RCSB], [http://www.ebi.ac.uk/pdbsum/4phr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4phr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/I1ZPA1_STRPA I1ZPA1_STRPA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Streptococcus parasanguinis fw213]] | + | [[Category: Streptococcus parasanguinis FW213]] |
| - | [[Category: Wu, H]] | + | [[Category: Wu H]] |
| - | [[Category: Zhang, H]] | + | [[Category: Zhang H]] |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
I1ZPA1_STRPA
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang H, Zhu F, Yang T, Ding L, Zhou M, Li J, Haslam SM, Dell A, Erlandsen H, Wu H. The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold. Nat Commun. 2014 Jul 15;5:4339. doi: 10.1038/ncomms5339. PMID:25023666 doi:http://dx.doi.org/10.1038/ncomms5339
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