|Biochemistry (2006) 45(48):14325-36|
|Center for Eukaryotic Structural Genomics|
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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.
|metabolism chemistry genetics enzymology classification |
|Binding Sites Crystallography, X-Ray Protein Structure, Tertiary Amino Acid Sequence Models, Molecular Molecular Sequence Data Protein Binding Sequence Alignment Catalysis Coenzyme A Sequence Homology, Amino Acid Nuclear Magnetic Resonance, Biomolecular Substrate Specificity Structural Homology, Protein Arabidopsis Histone Acetyltransferases Acetylation |
|6 (Last update: 10/13/2018 12:00:24pm)|
|multiple pdbids [1xmt,2evn]|