Structural highlights
4zxl is a 2 chain structure with sequence from Clop1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , |
| Related: | 2yds, 2ydr, 2ydq, 2vur |
| Gene: | nagJ, CPF_1442 (CLOP1) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[OGA_CLOP1] Biological function unknown. Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins.
Publication Abstract from PubMed
O-GlcNAcylation is a reversible type of serine/threonine glycosylation on nucleocytoplasmic proteins in metazoa. Various genetic approaches in several animal models have revealed that O-GlcNAcylation is essential for embryogenesis. However, the dynamic changes in global O-GlcNAcylation and the underlying mechanistic biology linking them to embryonic development is not understood. One of the limiting factors towards characterizing changes in O-GlcNAcylation has been the limited specificity of currently available tools to detect this modification. In the present study, harnessing the unusual properties of an O-GlcNAcase (OGA) mutant that binds O-GlcNAc (O-N-acetylglucosamine) sites with nanomolar affinity, we uncover changes in protein O-GlcNAcylation as a function of Drosophila development.
A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development.,Mariappa D, Selvan N, Borodkin V, Alonso J, Ferenbach AT, Shepherd C, Navratilova IH, vanAalten DMF Biochem J. 2015 Sep 1;470(2):255-262. doi: 10.1042/BJ20150610. Epub 2015 Jul 14. PMID:26348912[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Mariappa D, Selvan N, Borodkin V, Alonso J, Ferenbach AT, Shepherd C, Navratilova IH, vanAalten DMF. A mutant O-GlcNAcase as a probe to reveal global dynamics of protein O-GlcNAcylation during Drosophila embryonic development. Biochem J. 2015 Sep 1;470(2):255-262. doi: 10.1042/BJ20150610. Epub 2015 Jul 14. PMID:26348912 doi:http://dx.doi.org/10.1042/BJ20150610
