4NXY

Crystal Structure of the GNAT domain of S. lividans PAT

Summary for 4NXY

• Entry DOI: 10.2210/pdb4nxy/pdb
• Related: 1PG3 1PG4 4AVB
• Descriptor: Acyl-CoA synthetase, TRIFLUOROETHANOL, GLYCEROL, ... (4 entities in total)
• Functional Keywords: lysine acetyltransferase, amp-forming acetate:coa ligase enzyme (acs), transferase
• Biological source: Streptomyces lividans
• Total number of polymer chains: 1
• Total formula weight: 21845.40

Authors

Rank, K.C.,Tucker, A.C.,Escalante-Semerena, J.C.,Rayment, I. (deposition date: 2013-12-09, release date: 2014-11-19, Last modification date: 2024-02-28)

Primary citation

Tucker, A.C.,Taylor, K.C.,Rank, K.C.,Rayment, I.,Escalante-Semerena, J.C.
Insights into the specificity of lysine acetyltransferases.
J.Biol.Chem., 289:36249-36262, 2014

PubMed Abstract: 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 Å. 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.

PubMed: 25381442
DOI: 10.1074/jbc.M114.613901

Experimental method

X-RAY DIFFRACTION (1.449 Å)