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2bfr

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(New page: 200px<br /> <applet load="2bfr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bfr, resolution 2.5&Aring;" /> '''THE MACRO DOMAIN IS ...)
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[[Image:2bfr.gif|left|200px]]<br />
 
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<applet load="2bfr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2bfr, resolution 2.5&Aring;" />
 
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'''THE MACRO DOMAIN IS AN ADP-RIBOSE BINDING MODULE'''<br />
 
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==Overview==
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==The Macro domain is an ADP-ribose binding module==
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The ADP-ribosylation of proteins is an important post-translational, modification that occurs in a variety of biological processes, including, DNA repair, transcription, chromatin biology and long-term memory, formation. Yet no protein modules are known that specifically recognize, the ADP-ribose nucleotide. We provide biochemical and structural evidence, that macro domains are high-affinity ADP-ribose binding modules. Our, structural analysis reveals a conserved ligand binding pocket among the, macro domain fold. Consistently, distinct human macro domains retain their, ability to bind ADP-ribose. In addition, some macro domain proteins also, recognize poly-ADP-ribose as a ligand. Our data suggest an important role, for proteins containing macro domains in the biology of ADP-ribose.
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<StructureSection load='2bfr' size='340' side='right'caption='[[2bfr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bfr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BFR FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bfr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bfr OCA], [https://pdbe.org/2bfr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bfr RCSB], [https://www.ebi.ac.uk/pdbsum/2bfr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bfr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Y1521_ARCFU Y1521_ARCFU] Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Catalyzes removal of a phosphate group from ADP-ribose 1''-phosphate (Appr1p), but with low efficiency.<ref>PMID:23474712</ref> <ref>PMID:15902274</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/2bfr_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2bfr ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The ADP-ribosylation of proteins is an important post-translational modification that occurs in a variety of biological processes, including DNA repair, transcription, chromatin biology and long-term memory formation. Yet no protein modules are known that specifically recognize the ADP-ribose nucleotide. We provide biochemical and structural evidence that macro domains are high-affinity ADP-ribose binding modules. Our structural analysis reveals a conserved ligand binding pocket among the macro domain fold. Consistently, distinct human macro domains retain their ability to bind ADP-ribose. In addition, some macro domain proteins also recognize poly-ADP-ribose as a ligand. Our data suggest an important role for proteins containing macro domains in the biology of ADP-ribose.
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==About this Structure==
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The macro domain is an ADP-ribose binding module.,Karras GI, Kustatscher G, Buhecha HR, Allen MD, Pugieux C, Sait F, Bycroft M, Ladurner AG EMBO J. 2005 Jun 1;24(11):1911-20. Epub 2005 May 19. PMID:15902274<ref>PMID:15902274</ref>
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2BFR is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]] with MG and ADP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BFR OCA]].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The macro domain is an ADP-ribose binding module., Karras GI, Kustatscher G, Buhecha HR, Allen MD, Pugieux C, Sait F, Bycroft M, Ladurner AG, EMBO J. 2005 Jun 1;24(11):1911-20. Epub 2005 May 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15902274 15902274]
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</div>
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<div class="pdbe-citations 2bfr" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Archaeoglobus fulgidus]]
[[Category: Archaeoglobus fulgidus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Allen, M.D.]]
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[[Category: Allen MD]]
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[[Category: Buhecha, H.R.]]
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[[Category: Buhecha HR]]
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[[Category: Bycroft, M.]]
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[[Category: Bycroft M]]
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[[Category: Karras, G.I.]]
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[[Category: Karras GI]]
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[[Category: Ladurner, A.G.]]
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[[Category: Ladurner AG]]
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[[Category: Pugieux, C.]]
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[[Category: Pugieux C]]
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[[Category: Sait, F.]]
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[[Category: Sait F]]
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[[Category: ADP]]
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[[Category: MG]]
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[[Category: crystal structure p-loop]]
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[[Category: histone macroh2a]]
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[[Category: hydrolase]]
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[[Category: macro_h2a domain/hydrolase]]
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[[Category: nucleotide]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 19:42:46 2007''
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Current revision

The Macro domain is an ADP-ribose binding module

PDB ID 2bfr

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