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New page: left|200px<br /><applet load="1ii7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ii7, resolution 2.20Å" /> '''Crystal structure of...
 
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[[Image:1ii7.gif|left|200px]]<br /><applet load="1ii7" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ii7, resolution 2.20&Aring;" />
'''Crystal structure of P. furiosus Mre11 with manganese and dAMP'''<br />


==Overview==
==Crystal structure of P. furiosus Mre11 with manganese and dAMP==
To clarify functions of the Mre11/Rad50 (MR) complex in DNA double-strand, break repair, we report Pyrococcus furiosus Mre11 crystal structures, revealing a protein phosphatase-like, dimanganese binding domain capped by, a unique domain controlling active site access. These structures unify, Mre11's multiple nuclease activities in a single endo/exonuclease, mechanism and reveal eukaryotic macromolecular interaction sites by, mapping human and yeast Mre11 mutations. Furthermore, the structure of the, P. furiosus Rad50 ABC-ATPase with its adjacent coiled-coil defines a, compact Mre11/Rad50-ATPase complex and suggests that Rad50-ATP-driven, conformational switching directly controls the Mre11 exonuclease. Electron, microscopy, small angle X-ray scattering, and ultracentrifugation data of, human and P. furiosus MR reveal a dual functional complex consisting of a, (Mre11)2/(Rad50)2 heterotetrameric DNA processing head and a double, coiled-coil linker.
<StructureSection load='1ii7' size='340' side='right'caption='[[1ii7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ii7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1II7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1II7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D5M:2-DEOXYADENOSINE-5-MONOPHOSPHATE'>D5M</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1ii7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ii7 OCA], [https://pdbe.org/1ii7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ii7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ii7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ii7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MRE11_PYRFU MRE11_PYRFU] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity.
== 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/ii/1ii7_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=1ii7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
To clarify functions of the Mre11/Rad50 (MR) complex in DNA double-strand break repair, we report Pyrococcus furiosus Mre11 crystal structures, revealing a protein phosphatase-like, dimanganese binding domain capped by a unique domain controlling active site access. These structures unify Mre11's multiple nuclease activities in a single endo/exonuclease mechanism and reveal eukaryotic macromolecular interaction sites by mapping human and yeast Mre11 mutations. Furthermore, the structure of the P. furiosus Rad50 ABC-ATPase with its adjacent coiled-coil defines a compact Mre11/Rad50-ATPase complex and suggests that Rad50-ATP-driven conformational switching directly controls the Mre11 exonuclease. Electron microscopy, small angle X-ray scattering, and ultracentrifugation data of human and P. furiosus MR reveal a dual functional complex consisting of a (Mre11)2/(Rad50)2 heterotetrameric DNA processing head and a double coiled-coil linker.


==About this Structure==
Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase.,Hopfner KP, Karcher A, Craig L, Woo TT, Carney JP, Tainer JA Cell. 2001 May 18;105(4):473-85. PMID:11371344<ref>PMID:11371344</ref>
1II7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus] with PO4, MN, SO4 and DA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1II7 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase., Hopfner KP, Karcher A, Craig L, Woo TT, Carney JP, Tainer JA, Cell. 2001 May 18;105(4):473-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11371344 11371344]
</div>
<div class="pdbe-citations 1ii7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Pyrococcus furiosus]]
[[Category: Single protein]]
[[Category: Carney JP]]
[[Category: Carney, J.P.]]
[[Category: Craig L]]
[[Category: Craig, L.]]
[[Category: Hopfner K-P]]
[[Category: Hopfner, K.P.]]
[[Category: Karcher A]]
[[Category: Karcher, A.]]
[[Category: Tainer JA]]
[[Category: Tainer, J.A.]]
[[Category: Woo TT]]
[[Category: Woo, T.T.]]
[[Category: DA]]
[[Category: MN]]
[[Category: PO4]]
[[Category: SO4]]
[[Category: damp]]
[[Category: dna double-strand break repair]]
[[Category: manganese]]
[[Category: mre11]]
[[Category: rad50]]
 
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