The Crystal Structure of <i>Acanthamoeba Polyphaga</i> Mimivirus R655 and Its Potential Glycosaminoglycan Glycosyltransferase Activity.

ABSTRACT: Acanthamoeba polyphaga mimivirus (APMV) is a giant virus that encodes over 1,000 genes, many of which are involved in protein post-translational modifications, such as glycosylation. Here, we present the high-resolution crystal structure of a putative mimiviral glycosyltransferase R655 (Uniprot accession ID: Q5UQ62). R655 consists of a Rossmann domain with a glycosyltransferase family A (GT-A) fold followed by a CPW-WPC domain, connected by a long loop. The N-terminal region of this loop crosses over the Mn²⁺ and uridine diphosphate (UDP) binding pocket in the Rossmann domain, suggesting that it may function as a pocket cap. Within the binding pocket, the aspartate residue in the EXD motif coordinates Mn²⁺ while the glutamate residue is positioned to interact w

SUBMITTER: Kim JS 

PROVIDER: S-EPMC12710760 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature