1zr5: Difference between revisions

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[[Image:1zr5.png|left|200px]]
==Crystal structure of the macro-domain of human core histone variant macroH2A1.2==
<StructureSection load='1zr5' size='340' side='right' caption='[[1zr5]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1zr5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZR5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZR5 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zq0|1zq0]], [[1zr3|1zr3]]</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=1zr5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zr5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zr5 RCSB], [http://www.ebi.ac.uk/pdbsum/1zr5 PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zr/1zr5_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Histone macroH2A is a hallmark of mammalian heterochromatin. Here we show that human macroH2A1.1 binds the SirT1-metabolite O-acetyl-ADP-ribose (OAADPR) through its macro domain. The 1.6-A crystal structure and mutants reveal how the metabolite is recognized. Mutually exclusive exon use in the gene H2AFY produces macroH2A1.2, whose tissue distribution differs. MacroH2A1.2 shows only subtle structural changes but cannot bind nucleotides. Alternative splicing may thus regulate the binding of nicotinamide adenine dinucleotide (NAD) metabolites to chromatin.


{{STRUCTURE_1zr5|  PDB=1zr5  |  SCENE=  }}
Splicing regulates NAD metabolite binding to histone macroH2A.,Kustatscher G, Hothorn M, Pugieux C, Scheffzek K, Ladurner AG Nat Struct Mol Biol. 2005 Jul;12(7):624-5. Epub 2005 Jun 19. PMID:15965484<ref>PMID:15965484</ref>


===Crystal structure of the macro-domain of human core histone variant macroH2A1.2===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_15965484}}
 
==About this Structure==
[[1zr5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZR5 OCA].


==See Also==
==See Also==
*[[Histone|Histone]]
*[[Histone|Histone]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:015965484</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Hothorn, M.]]
[[Category: Hothorn, M.]]

Revision as of 07:19, 29 September 2014

Crystal structure of the macro-domain of human core histone variant macroH2A1.2Crystal structure of the macro-domain of human core histone variant macroH2A1.2

Structural highlights

1zr5 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:1zq0, 1zr3
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Histone macroH2A is a hallmark of mammalian heterochromatin. Here we show that human macroH2A1.1 binds the SirT1-metabolite O-acetyl-ADP-ribose (OAADPR) through its macro domain. The 1.6-A crystal structure and mutants reveal how the metabolite is recognized. Mutually exclusive exon use in the gene H2AFY produces macroH2A1.2, whose tissue distribution differs. MacroH2A1.2 shows only subtle structural changes but cannot bind nucleotides. Alternative splicing may thus regulate the binding of nicotinamide adenine dinucleotide (NAD) metabolites to chromatin.

Splicing regulates NAD metabolite binding to histone macroH2A.,Kustatscher G, Hothorn M, Pugieux C, Scheffzek K, Ladurner AG Nat Struct Mol Biol. 2005 Jul;12(7):624-5. Epub 2005 Jun 19. PMID:15965484[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Kustatscher G, Hothorn M, Pugieux C, Scheffzek K, Ladurner AG. Splicing regulates NAD metabolite binding to histone macroH2A. Nat Struct Mol Biol. 2005 Jul;12(7):624-5. Epub 2005 Jun 19. PMID:15965484 doi:http://dx.doi.org/10.1038/nsmb956

1zr5, resolution 2.92Å

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