1f1e
From Proteopedia
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|PDB= 1f1e |SIZE=350|CAPTION= <scene name='initialview01'>1f1e</scene>, resolution 1.37Å | |PDB= 1f1e |SIZE=350|CAPTION= <scene name='initialview01'>1f1e</scene>, resolution 1.37Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1e OCA], [http://www.ebi.ac.uk/pdbsum/1f1e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f1e RCSB]</span> | ||
}} | }} | ||
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[[Category: Lake, J A.]] | [[Category: Lake, J A.]] | ||
[[Category: Slesarev, A.]] | [[Category: Slesarev, A.]] | ||
| - | [[Category: CL]] | ||
[[Category: archaeal histone protein]] | [[Category: archaeal histone protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:13:54 2008'' |
Revision as of 17:13, 30 March 2008
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| , resolution 1.37Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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