1f1e: Difference between revisions

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-[[Image:1f1e.png|left|200px]]
+==CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI==
+<StructureSection load='1f1e' size='340' side='right' caption='[[1f1e]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1f1e]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F1E FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><br>
+<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1f1e RCSB], [http://www.ebi.ac.uk/pdbsum/1f1e PDBsum]</span></td></tr>
+<table>
+<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).
-{{STRUCTURE_1f1e|  PDB=1f1e  |  SCENE=  }}
+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>
-===CRYSTAL STRUCTURE OF THE HISTONE FROM METHANOPYRUS KANDLERI===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_11567091}}
-==About this Structure==
-[[1f1e]] is a 1 chain structure with 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].
 ==See Also==
 *[[Histone|Histone]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:011567091</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Methanopyrus kandleri]]
 [[Category: Cascio, D.]]