4nxy | pdb_00004nxy

Crystal Structure of the GNAT domain of S. lividans PAT

spinqualitylabelsall models 4nxy, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nxy is a 1 chain structure with sequence from Streptomyces lividans TK24. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ETF, GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA