Summary for 2EVN
| Entry DOI | 10.2210/pdb2evn/pdb |
| NMR Information | BMRB: 6338 |
| Descriptor | Protein At1g77540 (1 entity in total) |
| Functional Keywords | psi structural genomics cesg at1g77540 center for eukaryotic structural genomics, protein structure initiative, structural genomics, unknown function |
| Biological source | Arabidopsis thaliana (thale cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 11752.43 |
| Authors | Tyler, R.C.,Singh, S.,Tonelli, M.,Min, M.S.,Markley, J.L.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2005-10-31, release date: 2005-11-15, Last modification date: 2024-05-22) |
| Primary citation | Tyler, R.C.,Bitto, E.,Berndsen, C.E.,Bingman, C.A.,Singh, S.,Lee, M.S.,Wesenberg, G.E.,Denu, J.M.,Phillips Jr., G.N.,Markley, J.L. Structure of Arabidopsis thaliana At1g77540 Protein, a Minimal Acetyltransferase from the COG2388 Family. Biochemistry, 45:14325-14336, 2006 Cited by PubMed Abstract: We describe X-ray crystal and NMR solution structures of the protein coded for by Arabidopsis thaliana gene At1g77540.1 (At1g77540). The crystal structure was determined to 1.15 A with an R factor of 14.9% (Rfree = 17.0%) by multiple-wavelength anomalous diffraction using sodium bromide derivatized crystals. The ensemble of NMR conformers was determined with protein samples labeled with 15N and 13C + 15N. The X-ray structure and NMR ensemble were closely similar with rmsd 1.4 A for residues 8-93. At1g77540 was found to adopt a fold similar to that of GCN5-related N-acetyltransferases. Enzymatic activity assays established that At1g77540 possesses weak acetyltransferase activity against histones H3 and H4. Chemical shift perturbations observed in 15N-HSQC spectra upon the addition of CoA indicated that the cofactor binds and identified its binding site. The molecular details of this interaction were further elucidated by solving the X-ray structure of the At1g77540-CoA complex. This work establishes that the domain family COG2388 represents a novel class of acetyltransferase and provides insight into possible mechanistic roles of the conserved Cys76 and His41 residues of this family. PubMed: 17128971DOI: 10.1021/bi0612059 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
