View source for 2bud


==The solution structure of the chromo barrel domain from the males- absent on the first (MOF) protein==
<StructureSection load='2bud' size='340' side='right'caption='[[2bud]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bud]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BUD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2bud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bud OCA], [https://pdbe.org/2bud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bud RCSB], [https://www.ebi.ac.uk/pdbsum/2bud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bud ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MOF_DROME MOF_DROME] Histone acetyltransferase that plays a direct role in the specific histone acetylation associated with dosage compensation as part of the male-specific lethal (MSL) complex (PubMed:9155031, PubMed:16543150, PubMed:34133927). Dosage compensation insures that males with a single X chromosome have the same amount of most X-linked gene products as females with two X chromosomes (PubMed:9155031). May be directly involved in the acetylation of histone 4 at 'Lys-16' on the X chromosome of males where it is recruited by the MSL complex (PubMed:11258702). As part of the nonspecific lethal (NLS) complex may associate with promoters of X chromosomal as well as autosomal genes and positively regulate their transcription through chromatin modification (PubMed:20620954).<ref>PMID:11258702</ref> <ref>PMID:16543150</ref> <ref>PMID:20620954</ref> <ref>PMID:34133927</ref> <ref>PMID:9155031</ref> 
== 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/bu/2bud_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/main_output.php?pdb_ID=2bud ConSurf].
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== Publication Abstract from PubMed ==
We report here the structure of the putative chromo domain from MOF, a member of the MYST family of histone acetyltransferases that acetylates histone H4 at Lys-16 and is part of the dosage compensation complex in Drosophila. We found that the structure of this domain is a beta-barrel that is distinct from the alpha + beta fold of the canonical chromo domain. Despite the differences, there are similarities that support an evolutionary relationship between the two domains, and we propose the name "chromo barrel." The chromo barrel domains may be divided into two groups, MSL3-like and MOF-like, on the basis of whether a group of conserved aromatic residues is present or not. The structure suggests that, although the MOF-like domains may have a role in RNA binding, the MSL3-like domains could instead bind methylated residues. The MOF chromo barrel shares a common fold with other chromatin-associated modules, including the MBT-like repeat, Tudor, and PWWP domains. This structural similarity suggests a probable evolutionary pathway from these other modules to the canonical chromo domains (or vice versa) with the chromo barrel domain representing an intermediate structure.

Structure of the chromo barrel domain from the MOF acetyltransferase.,Nielsen PR, Nietlispach D, Buscaino A, Warner RJ, Akhtar A, Murzin AG, Murzina NV, Laue ED J Biol Chem. 2005 Sep 16;280(37):32326-31. Epub 2005 Jun 17. PMID:15964847<ref>PMID:15964847</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2bud" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Akhtar A]]
[[Category: Buscaino A]]
[[Category: Laue ED]]
[[Category: Murzin AG]]
[[Category: Murzina NV]]
[[Category: Nielsen PR]]
[[Category: Nietlispach D]]
[[Category: Warner RJ]]