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4Z9E

Alba from Thermoplasma volcanium

Summary for 4Z9E
Entry DOI10.2210/pdb4z9e/pdb
DescriptorDNA/RNA-binding protein Alba (2 entities in total)
Functional Keywordsthermoplasma volcanium, acetyltransferase, dna binding protein
Biological sourceThermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Cellular locationCytoplasm : Q979S5
Total number of polymer chains4
Total formula weight44206.35
Authors
Ma, C.,Lee, S.J.,Pathak, C.,Lee, B.J. (deposition date: 2015-04-10, release date: 2016-02-24, Last modification date: 2023-11-08)
Primary citationMa, C.,Pathak, C.,Lee, S.J.,Lee, K.Y.,Jang, S.B.,Nam, M.,Im, H.,Yoon, H.J.,Lee, B.J.
Alba from Thermoplasma volcanium belongs to alpha-NAT's: An insight into the structural aspects of Tv Alba and its acetylation by Tv Ard1.
Arch.Biochem.Biophys., 590:90-100, 2016
Cited by
PubMed Abstract: The Alba superfamily proteins have been regarded as a conserved group of proteins in archaea and eukarya, which have shown to be important in nucleic acid binding, chromatic organization and gene regulation. These proteins often belong to the N-acetyltransferase (NAT) category (N(α)-acetyltransferases or N(ε)-acetyltransferases) and undergo post-translational modifications. Here, we report the crystal structure of Alba from Thermoplasma volcanium (Tv Alba) at 2.4 Å resolution. The acetylation of Tv Alba was monitored and the N-terminal of Tv Alba has been shown to interact with acetyl coenzyme A (Ac-CoA). The chemical shift perturbation experiments of Tv Alba were performed in the presence of Ac-CoA and/or Tv Ard1, another T. volcanium protein that treats Tv Alba as a substrate. To examine the DNA binding capabilities of Tv Alba alone and in the presence of Ac-CoA and/or Tv Ard1, EMSA experiments were carried out. It is shown that although Tv Alba binds to Ac-CoA, the acetylation of Tv Alba is not related with its binding to dsDNA, and the involvement of the N-terminus in Ac-CoA binding demonstrates that Tv Alba belongs to the N(α)-acetyltransferase family.
PubMed: 26657068
DOI: 10.1016/j.abb.2015.11.039
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.49 Å)
Structure validation

237735

数据于2025-06-18公开中

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