View source for 2xr1


==DIMERIC ARCHAEAL CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR WITH N-TERMINAL KH DOMAINS (KH-CPSF) FROM METHANOSARCINA MAZEI==
<StructureSection load='2xr1' size='340' side='right'caption='[[2xr1]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2xr1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei Methanosarcina mazei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XR1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XR1 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]] 2.59&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2xr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xr1 OCA], [https://pdbe.org/2xr1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xr1 RCSB], [https://www.ebi.ac.uk/pdbsum/2xr1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xr1 ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/Q8PZ03_METMA Q8PZ03_METMA] 
== 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/xr/2xr1_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=2xr1 ConSurf].
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== Publication Abstract from PubMed ==
Proteins of the metallo-beta-lactamase (MbetaL) fold form a large superfamily of metallo-hydrolase/oxidoreductases. Members of this family are found in all three domains of life and are involved in a variety of biological functions related to hydrolysis, redox processes, DNA repair and uptake, and RNA processing. We classified the archaeal homologs of this superfamily based on sequence similarity and characterized a subfamily of the Cleavage and Polyadenylation Specificity Factor (CPSF) with an uncommon domain composition: in addition to an extended MbetaL domain, which accommodates the active site for RNA cleavage, this group has two N-terminal KH domains. Here, we present the crystal structure of a member of this group from Methanosarcina mazei. It reveals a dimerization mode of the MbetaL domain that has not been observed before and suggests that RNA is bound across the dimer interface, recognized by the KH domains of one monomer, and cleaved at the active site of the other.

Crystal structure of a dimeric archaeal Cleavage and Polyadenylation Specificity Factor.,Mir-Montazeri B, Ammelburg M, Forouzan D, Lupas AN, Hartmann MD J Struct Biol. 2010 Sep 17. PMID:20851187<ref>PMID:20851187</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 2xr1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanosarcina mazei]]
[[Category: Ammelburg M]]
[[Category: Forouzan D]]
[[Category: Hartmann MD]]
[[Category: Lupas AN]]
[[Category: Mir-Montazeri B]]