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4PHR

Domain of unknown function 1792 (DUF1792) with manganese

Summary for 4PHR
Entry DOI10.2210/pdb4phr/pdb
Related4PFX 4PHS
DescriptorPutative glycosyltransferase (GalT1), URIDINE-5'-DIPHOSPHATE, MANGANESE (II) ION, ... (5 entities in total)
Functional Keywordsdomain of unknown function 1792 (duf1792), glycosyltransferase, transferase
Biological sourceStreptococcus parasanguinis
Total number of polymer chains1
Total formula weight32722.75
Authors
Zhang, H.,Wu, H. (deposition date: 2014-05-06, release date: 2014-08-06, Last modification date: 2023-12-27)
Primary citationZhang, H.,Zhu, F.,Yang, T.,Ding, L.,Zhou, M.,Li, J.,Haslam, S.M.,Dell, A.,Erlandsen, H.,Wu, H.
The highly conserved domain of unknown function 1792 has a distinct glycosyltransferase fold.
Nat Commun, 5:4339-4339, 2014
Cited by
PubMed Abstract: 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-Å 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.
PubMed: 25023666
DOI: 10.1038/ncomms5339
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.34 Å)
Structure validation

238582

数据于2025-07-09公开中

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