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| {{STRUCTURE_1f1e| PDB=1f1e | SCENE= }} | | {{STRUCTURE_1f1e| PDB=1f1e | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI'''
| | ===CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI=== |
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| ==Overview==
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| 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).
| | The line below this paragraph, {{ABSTRACT_PUBMED_11567091}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11567091 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11567091}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Slesarev, A.]] | | [[Category: Slesarev, A.]] |
| [[Category: Archaeal histone protein]] | | [[Category: Archaeal histone protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:46:36 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:20:17 2008'' |