1F1E

CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI

Summary for 1F1E

• Entry DOI: 10.2210/pdb1f1e/pdb
• Descriptor: HISTONE FOLD PROTEIN, CHLORIDE ION (3 entities in total)
• Functional Keywords: archaeal histone protein, dna binding protein
• Biological source: Methanopyrus kandleri
• Total number of polymer chains: 1
• Total formula weight: 17250.34

Authors

Fahrner, R.L.,Cascio, D.,Lake, J.A.,Slesarev, A. (deposition date: 2000-05-18, release date: 2001-10-31, Last modification date: 2024-10-30)

Primary citation

Fahrner, R.L.,Cascio, D.,Lake, J.A.,Slesarev, A.
An ancestral nuclear protein assembly: crystal structure of the Methanopyrus kandleri histone.
Protein Sci., 10:2002-2007, 2001

PubMed Abstract: Eukaryotic histone proteins condense DNA into compact structures called nucleosomes. Nucleosomes were viewed as a distinguishing feature of eukaryotes prior to identification of histone orthologs in methanogens. Although evolutionarily distinct from methanogens, the methane-producing hyperthermophile Methanopyrus kandleri produces a novel, 154-residue histone (HMk). Amino acid sequence comparisons show that HMk differs from both methanogenic and eukaryotic histones, in that it contains two histone-fold ms within a single chain. The two HMk histone-fold ms, N and C terminal, are 28% identical in amino acid sequence to each other and approximately 21% identical in amino acid sequence to other histone proteins. Here we present the 1.37-A-resolution crystal structure of HMk and report that the HMk monomer structure is homologous to the eukaryotic histone heterodimers. In the crystal, HMk forms a dimer homologous to [H3-H4](2) in the eukaryotic nucleosome. Based on the spatial similarities to structural ms found in the eukaryotic nucleosome that are important for DNA-binding, we infer that the Methanopyrus histone binds DNA in a manner similar to the eukaryotic histone tetramer [H3-H4](2).

PubMed: 11567091
DOI: 10.1110/ps.10901

Experimental method

X-RAY DIFFRACTION (1.37 Å)