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   An ancestral nuclear protein assembly: crystal structure of the
   Methanopyrus kandleri histone.
   (PMID:11567091)
     * [23]Abstract This article is available in UKPMC
     * [24]Citations List of citations in UKPMC which this record is cited
       by and<br/> those which it cites
     * [25]BioEntities Biological entities annotated by the EMBL EBI and
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       words in the title and abstract

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   [28]Fahrner RL,
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   [30]Cascio D,
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   [32]Lake JA,
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   [34]Slesarev A
   Department of Chemistry and Biochemistry, University of California, Los
   Angeles, California 90095-1570, USA.
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   [36]Protein Science : a Publication of the Protein Society [2001,
   10(10):2002-7]

   Type:  Journal Article, Comparative Study

   DOI: 10.1110/ps.10901 The Digital Object Identifier (DOI) System
   enables identification of digital entities
   Abstract Highlight Terms Highlight biological terms.
   [ ] Gene Ontology(2) [ ] Species(3)

   Eukaryotic histone proteins condense DNA into compact structures called
   [37]nucleosomes. [38]Nucleosomes were viewed as a distinguishing
   feature of [39]eukaryotes prior to identification of histone orthologs
   in methanogens. Although evolutionarily distinct from methanogens, the
   methane-producing hyperthermophile [40]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 [41]nucleosome. Based on the spatial similarities to
   structural ms found in the eukaryotic [42]nucleosome that are important
   for [43]DNA-binding, we infer that the [44]Methanopyrus histone binds
   DNA in a manner similar to the eukaryotic histone tetramer [H3-H4](2).
   [45]Read Article at www.proteinscience.org (Subscription required)
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