ArticleActa crystallographica. Section D, Biological crystallography2014
Three-dimensional structure of a Streptomyces sviceus GNAT acetyltransferase with similarity to the C-terminal domain of the human GH84 O-GlcNAcase.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 34 citations in OpenAlex.
- Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms.Nature communications · 2025Article
- Review
- Review
- Complex Crystal Structure Determination of Hsp90Frontiers in oncology · 2022Article
- The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape.Genes · 2021Review
- OGA is associated with deglycosylation of NONO and the KU complex during DNA damage repair.Cell death & disease · 2021Article
- Complex Crystal Structure Determination andFrontiers in cell and developmental biology · 2021Article
- Molecular Interrogation to Crack the Case of O-GlcNAc.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Review
- Article
- O-GlcNAcylation in immunity and inflammation: An intricate system (Review).International journal of molecular medicine · 2019Review
- Cell Metabolism Control Through O-GlcNAcylation of STAT5: A Full or Empty Fuel Tank Makes a Big Difference for Cancer Cell Growth and Survival.International journal of molecular sciences · 2019Review
- Chemical and Biochemical Strategies To Explore the Substrate Recognition of O-GlcNAc-Cycling Enzymes.Chembiochem : a European journal of chemical biology · 2019Review
- Structural studies of a surface-entropy reduction mutant of O-GlcNAcase.Acta crystallographica. Section D, Structural biology · 2019Article
- Critical observations that shaped our understanding of the function(s) of intracellular glycosylation (O-GlcNAc).FEBS letters · 2018Review
- O-Linked β-Clinical science (London, England : 1979) · 2018Review
- O-GlcNAcylation and neurodegeneration.Brain research bulletin · 2017Review
- Structures of human O-GlcNAcase and its complexes reveal a new substrate recognition mode.Nature structural & molecular biology · 2017Article
- N-acetylglucosamine sensing by a GCN5-related N-acetyltransferase induces transcription via chromatin histone acetylation in fungi.Nature communications · 2016Article
- A unique GCN5-related glucosamine N-acetyltransferase region exist in the fungal multi-domain glycoside hydrolase family 3 β-N-acetylglucosaminidase.Scientific reports · 2015Article
- You are what you eat: O-linked N-acetylglucosamine in disease, development and epigenetics.Current opinion in clinical nutrition and metabolic care · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The mammalian O-GlcNAc hydrolysing enzyme O-GlcNAcase (OGA) is a multi-domain protein with glycoside hydrolase activity in the N-terminus and with a C-terminal domain that has low sequence similarity to known acetyltransferases, prompting speculation, albeit controversial, that the C-terminal domain may function as a histone acetyltransferase (HAT). There are currently scarce data available regarding the structure and function of this C-terminal region. Here, a bacterial homologue of the human OGA C-terminal domain, an acetyltransferase protein (accession No. ZP_05014886) from Streptomyces sviceus (SsAT), was cloned and its crystal structure was solved to high resolution. The structure reveals a conserved protein core that has considerable structural homology to the acetyl-CoA (AcCoA) binding site of GCN5-related acetyltransferases (GNATs). Calorimetric data further confirm that SsAT is indeed able to bind AcCoA in solution with micromolar affinity. Detailed structural analysis provided insight into the binding of AcCoA. An acceptor-binding cavity was identified, indicating that the physiological substrate of SsAT may be a small molecule. Consistent with recently published work, the SsAT structure further questions a HAT function for the human OGA domain.
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Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.