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| | <StructureSection load='4nxy' size='340' side='right'caption='[[4nxy]], [[Resolution|resolution]] 1.45Å' scene=''> | | <StructureSection load='4nxy' size='340' side='right'caption='[[4nxy]], [[Resolution|resolution]] 1.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4nxy]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans_tk24 Streptomyces lividans tk24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NXY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NXY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nxy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans_TK24 Streptomyces lividans TK24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NXY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NXY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ETF:TRIFLUOROETHANOL'>ETF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ETF:TRIFLUOROETHANOL'>ETF</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pg3|1pg3]], [[1pg4|1pg4]], [[4avb|4avb]]</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=4nxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nxy OCA], [https://pdbe.org/4nxy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nxy RCSB], [https://www.ebi.ac.uk/pdbsum/4nxy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nxy ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SSPG_01886 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=457428 Streptomyces lividans TK24])</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=4nxy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nxy OCA], [http://pdbe.org/4nxy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nxy RCSB], [http://www.ebi.ac.uk/pdbsum/4nxy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nxy ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Streptomyces lividans tk24]] | + | [[Category: Streptomyces lividans TK24]] |
| - | [[Category: Escalante-Semerena, J C]] | + | [[Category: Escalante-Semerena JC]] |
| - | [[Category: Rank, K C]] | + | [[Category: Rank KC]] |
| - | [[Category: Rayment, I]] | + | [[Category: Rayment I]] |
| - | [[Category: Tucker, A C]] | + | [[Category: Tucker AC]] |
| - | [[Category: Lysine acetyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Reversible lysine acetylation by protein acetyltransferases is a conserved regulatory mechanism that controls diverse cellular pathways. Gcn5-related N-acetyltransferases (GNATs), named after their founding member, are found in all domains of life. GNATs are known for their role as histone acetyltransferases, but non-histone bacterial protein acetytransferases have been identified. Only structures of GNAT complexes with short histone peptide substrates are available in databases. Given the biological importance of this modification and the abundance of lysine in polypeptides, how specificity is attained for larger protein substrates is central to understanding acetyl-lysine regulated networks. Here we report the structure of a GNAT in complex with a globular protein substrate solved to 1.9 Angstrom. GNAT binds the protein substrate with extensive surface interactions distinct from those reported for GNAT-peptide complexes. Our data reveal determinants needed for the recognition of a protein substrate and provide insight into the specificity of GNATs.
Insights Into the Specificity of Lysine Acetyltransferases.,Tucker AC, Taylor KC, Rank KC, Rayment I, Escalante-Semerena JC J Biol Chem. 2014 Nov 7. pii: jbc.M114.613901. PMID:25381442[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tucker AC, Taylor KC, Rank KC, Rayment I, Escalante-Semerena JC. Insights Into the Specificity of Lysine Acetyltransferases. J Biol Chem. 2014 Nov 7. pii: jbc.M114.613901. PMID:25381442 doi:http://dx.doi.org/10.1074/jbc.M114.613901
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