1f1e
From Proteopedia
(New page: 200px<br /><applet load="1f1e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f1e, resolution 1.37Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1f1e.gif|left|200px]]<br /><applet load="1f1e" size=" | + | [[Image:1f1e.gif|left|200px]]<br /><applet load="1f1e" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1f1e, resolution 1.37Å" /> | caption="1f1e, resolution 1.37Å" /> | ||
'''CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI'''<br /> | '''CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Eukaryotic histone proteins condense DNA into compact structures called | + | 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== | ==About this Structure== | ||
| - | 1F1E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1F1E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1E OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cascio, D.]] | [[Category: Cascio, D.]] | ||
| - | [[Category: Fahrner, R | + | [[Category: Fahrner, R L.]] |
| - | [[Category: Lake, J | + | [[Category: Lake, J A.]] |
[[Category: Slesarev, A.]] | [[Category: Slesarev, A.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
[[Category: archaeal histone protein]] | [[Category: archaeal histone protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:46 2008'' |
Revision as of 10:33, 21 February 2008
|
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 with as ligand. 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
Page seeded by OCA on Thu Feb 21 12:33:46 2008
