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  Three-dimensional structure of a Streptomyces sviceus GNAT acetyltransferase with similarity to the C-terminal domain of the human GH84 O-GlcNAcase

He, Y., Roth, C., Turkenburg, J. P., & Davies, G. J. (2014). Three-dimensional structure of a Streptomyces sviceus GNAT acetyltransferase with similarity to the C-terminal domain of the human GH84 O-GlcNAcase. Acta Crystallographica Section D, 70(1), 186-195. doi:10.1107/S1399004713029155.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-24EE-C Version Permalink: http://hdl.handle.net/21.11116/0000-0000-24EF-B
Genre: Journal Article

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 Creators:
He, Yuan, Author
Roth, Christian1, Author              
Turkenburg, Johan P., Author
Davies, Gideon J., Author
Affiliations:
1External Organizations, ou_persistent22              

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Free keywords: acetyltransferases, O-GlcNAc, GCN5, GNAT, acetyl-CoA
 Abstract: The mammalian ıt O}-GlcNAc hydrolysing enzyme {ıt 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 {ıt 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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 Dates: 2014-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1107/S1399004713029155
BibTex Citekey: He:dz5307
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Title: Acta Crystallographica Section D
  Other : Acta Crystallogr D
Source Genre: Journal
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Publ. Info: [Copenhagen, Denmark : Published for the International Union of Crystallography by Munksgaard]
Pages: - Volume / Issue: 70 (1) Sequence Number: - Start / End Page: 186 - 195 Identifier: ISSN: 0907-4449