1f1e: Difference between revisions
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==CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI== | |||
<StructureSection load='1f1e' size='340' side='right'caption='[[1f1e]], [[Resolution|resolution]] 1.37Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1f1e]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F1E FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.37Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1e OCA], [https://pdbe.org/1f1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f1e RCSB], [https://www.ebi.ac.uk/pdbsum/1f1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f1e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/O93641_9EURY O93641_9EURY] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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). | |||
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<ref>PMID:11567091</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1f1e" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Histone|Histone]] | *[[Histone 3D structures|Histone 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methanopyrus kandleri]] | [[Category: Methanopyrus kandleri]] | ||
[[Category: Cascio | [[Category: Cascio D]] | ||
[[Category: Fahrner | [[Category: Fahrner RL]] | ||
[[Category: Lake | [[Category: Lake JA]] | ||
[[Category: Slesarev | [[Category: Slesarev A]] | ||