4NXY

Crystal Structure of the GNAT domain of S. lividans PAT

4NXY の概要

• エントリーDOI: 10.2210/pdb4nxy/pdb
• 関連するPDBエントリー: 1PG3 1PG4 4AVB
• 分子名称: Acyl-CoA synthetase, TRIFLUOROETHANOL, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: lysine acetyltransferase, amp-forming acetate:coa ligase enzyme (acs), transferase
• 由来する生物種: Streptomyces lividans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21845.40

構造登録者

Rank, K.C.,Tucker, A.C.,Escalante-Semerena, J.C.,Rayment, I. (登録日: 2013-12-09, 公開日: 2014-11-19, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.449 Å)