3oa6: Difference between revisions

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==Human MSL3 Chromodomain bound to DNA and H4K20me1 peptide==
==Human MSL3 Chromodomain bound to DNA and H4K20me1 peptide==
<StructureSection load='3oa6' size='340' side='right' caption='[[3oa6]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='3oa6' size='340' side='right' caption='[[3oa6]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3oa6]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3m9p 3m9p]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OA6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3oa6]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3m9p 3m9p]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OA6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLZ:N-METHYL-LYSINE'>MLZ</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m9q|3m9q]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3m9q|3m9q]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSL3, MSL3L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSL3, MSL3L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oa6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oa6 RCSB], [http://www.ebi.ac.uk/pdbsum/3oa6 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oa6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oa6 OCA], [http://pdbe.org/3oa6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3oa6 RCSB], [http://www.ebi.ac.uk/pdbsum/3oa6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3oa6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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].
</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=3oa6 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3oa6" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Human]]
[[Category: Huang, P]]
[[Category: Huang, P]]
[[Category: Khorasanizadeh, S]]
[[Category: Khorasanizadeh, S]]

Latest revision as of 17:04, 4 August 2016

Human MSL3 Chromodomain bound to DNA and H4K20me1 peptideHuman MSL3 Chromodomain bound to DNA and H4K20me1 peptide

Structural highlights

3oa6 is a 7 chain structure with sequence from Human. This structure supersedes the now removed PDB entry 3m9p. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Gene:MSL3, MSL3L1 (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MS3L1_HUMAN] May be involved in chromatin remodeling and transcriptional regulation. May have a role in X inactivation. Component of the MSL complex which is responsible for the majority of histone H4 acetylation at 'Lys-16' which is implicated in the formation of higher-order chromatin structure. Specifically recognizes histone H4 monomethylated at 'Lys-20' (H4K20Me1) in a DNA-dependent manner and is proposed to be involved in chromosomal targeting of the MSL complex.[1] [2] [3] [4]

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

MSL3 resides in the MSL (male-specific lethal) complex, which upregulates transcription by spreading the histone H4 Lys16 (H4K16) acetyl mark. We discovered a DNA-dependent interaction of MSL3 chromodomain with the H4K20 monomethyl mark. The structure of a ternary complex shows that the DNA minor groove accommodates the histone H4 tail, and monomethyllysine inserts in a four-residue aromatic cage in MSL3. H4K16 acetylation antagonizes MSL3 binding, suggesting that MSL function is regulated by a combination of post-translational modifications.

Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain.,Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587[5]

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

References

  1. ↑ Smith ER, Cayrou C, Huang R, Lane WS, Cote J, Lucchesi JC. A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Mol Cell Biol. 2005 Nov;25(21):9175-88. PMID:16227571 doi:10.1128/MCB.25.21.9175-9188.2005
  2. ↑ Cai Y, Jin J, Swanson SK, Cole MD, Choi SH, Florens L, Washburn MP, Conaway JW, Conaway RC. Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex. J Biol Chem. 2010 Feb 12;285(7):4268-72. doi: 10.1074/jbc.C109.087981. Epub 2009 , Dec 14. PMID:20018852 doi:10.1074/jbc.C109.087981
  3. ↑ Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain. Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587 doi:10.1038/nsmb.1856
  4. ↑ Moore SA, Ferhatoglu Y, Jia Y, Al-Jiab RA, Scott MJ. Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4. J Biol Chem. 2010 Dec 24;285(52):40879-90. doi: 10.1074/jbc.M110.134312. Epub, 2010 Oct 12. PMID:20943666 doi:10.1074/jbc.M110.134312
  5. ↑ Kim D, Blus BJ, Chandra V, Huang P, Rastinejad F, Khorasanizadeh S. Corecognition of DNA and a methylated histone tail by the MSL3 chromodomain. Nat Struct Mol Biol. 2010 Aug;17(8):1027-9. Epub 2010 Jul 25. PMID:20657587 doi:10.1038/nsmb.1856

3oa6, resolution 2.35Å

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