1f1e
From Proteopedia
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| - | [[Image:1f1e.gif|left|200px]] | + | [[Image:1f1e.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI''' | + | {{Structure |
| + | |PDB= 1f1e |SIZE=350|CAPTION= <scene name='initialview01'>1f1e</scene>, resolution 1.37Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F1E is a [ | + | 1F1E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1E OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11567091 11567091] |
[[Category: Methanopyrus kandleri]] | [[Category: Methanopyrus kandleri]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: archaeal histone protein]] | [[Category: archaeal histone protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:07 2008'' |
Revision as of 09:03, 20 March 2008
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| , resolution 1.37Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI
Overview
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 Structure
1F1E is a Single protein structure of sequence from Methanopyrus kandleri. Full crystallographic information is available from OCA.
Reference
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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