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1XMT

X-ray structure of gene product from arabidopsis thaliana at1g77540

Summary for 1XMT
Entry DOI10.2210/pdb1xmt/pdb
Descriptorputative acetyltransferase, BROMIDE ION (3 entities in total)
Functional Keywordsstructural genomics, protein structure initiative, cesg, at1g77540, putative acetyltransferase, psi, center for eukaryotic structural genomics, unknown function
Biological sourceArabidopsis thaliana (thale cress)
Total number of polymer chains1
Total formula weight12587.26
Authors
Wesenberg, G.E.,Smith, D.W.,Phillips Jr., G.N.,Bitto, E.,Bingman, C.A.,Allard, S.T.M.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2004-10-04, release date: 2004-10-12, Last modification date: 2024-02-14)
Primary citationTyler, 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: 17128971
DOI: 10.1021/bi0612059
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.15 Å)
Structure validation

226707

數據於2024-10-30公開中

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