4bmh
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | + | ==Crystal structure of SsHAT== | |
| - | === | + | <StructureSection load='4bmh' size='340' side='right' caption='[[4bmh]], [[Resolution|resolution]] 1.50Å' scene=''> |
| - | + | == 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> | ||
| + | </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> | ||
| + | <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://www.rcsb.org/pdb/explore.do?structureId=4bmh RCSB], [http://www.ebi.ac.uk/pdbsum/4bmh PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:24419391</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| - | [[Category: Davies, G J | + | == References == |
| - | [[Category: He, Y | + | <references/> |
| - | [[Category: Turkenburg, J P | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Streptomyces sviceus atcc 29083]] | ||
| + | [[Category: Davies, G J]] | ||
| + | [[Category: He, Y]] | ||
| + | [[Category: Turkenburg, J P]] | ||
[[Category: Hat]] | [[Category: Hat]] | ||
[[Category: O-glcnacase]] | [[Category: O-glcnacase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 18:53, 21 December 2014
Crystal structure of SsHAT
| |||||||||||
