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| | <StructureSection load='4bmh' size='340' side='right'caption='[[4bmh]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='4bmh' size='340' side='right'caption='[[4bmh]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bmh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_sviceus_atcc_29083 Streptomyces sviceus atcc 29083]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BMH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BMH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bmh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sviceus_ATCC_29083 Streptomyces sviceus ATCC 29083]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BMH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bmh OCA], [http://pdbe.org/4bmh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bmh RCSB], [http://www.ebi.ac.uk/pdbsum/4bmh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bmh ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> |
| | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bmh OCA], [https://pdbe.org/4bmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bmh RCSB], [https://www.ebi.ac.uk/pdbsum/4bmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bmh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/B5HKU0_9ACTN B5HKU0_9ACTN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Streptomyces sviceus atcc 29083]] | + | [[Category: Streptomyces sviceus ATCC 29083]] |
| - | [[Category: Davies, G J]] | + | [[Category: Davies GJ]] |
| - | [[Category: He, Y]] | + | [[Category: He Y]] |
| - | [[Category: Turkenburg, J P]] | + | [[Category: Turkenburg JP]] |
| - | [[Category: Hat]]
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| - | [[Category: O-glcnacase]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
B5HKU0_9ACTN
Publication Abstract from PubMed
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.
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 JP, Davies GJ Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):186-95. doi:, 10.1107/S1399004713029155. Epub 2013 Dec 31. PMID:24419391[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ He Y, Roth C, Turkenburg JP, Davies GJ. Three-dimensional structure of a Streptomyces sviceus GNAT acetyltransferase with similarity to the C-terminal domain of the human GH84 O-GlcNAcase. Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):186-95. doi:, 10.1107/S1399004713029155. Epub 2013 Dec 31. PMID:24419391 doi:http://dx.doi.org/10.1107/S1399004713029155
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