1f1e
CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI
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OverviewOverview
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).
About this StructureAbout this Structure
1F1E is a Single protein structure of sequence from Methanopyrus kandleri with CL as ligand. Full crystallographic information is available from OCA.
ReferenceReference
An ancestral nuclear protein assembly: crystal structure of the Methanopyrus kandleri histone., Fahrner RL, Cascio D, Lake JA, Slesarev A, Protein Sci. 2001 Oct;10(10):2002-7. PMID:11567091
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