2ycb: Difference between revisions

<StructureSection load='2ycb' size='340' side='right'caption='[[2ycb]], [[Resolution|resolution]] 3.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[2ycb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus_str._Delta_H Methanothermobacter thermautotrophicus str. Delta H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YCB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YCB 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]] 3.1&#8491;</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <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=2ycb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ycb OCA], [https://pdbe.org/2ycb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ycb RCSB], [https://www.ebi.ac.uk/pdbsum/2ycb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ycb ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

MTH1203, a beta-CASP metallo-beta-lactamase family nuclease from the archaeon Methanothermobacter thermautotrophicus, was identified as a putative nuclease that might contribute to RNA processing. The crystal structure of MTH1203 reveals that, in addition to the metallo-beta-lactamase nuclease and the beta-CASP domains, it contains two contiguous KH domains that are unique to MTH1203 and its orthologs. RNA-binding experiments indicate that MTH1203 preferentially binds U-rich sequences with a dissociation constant in the micromolar range. In vitro nuclease activity assays demonstrated that MTH1203 is a zinc-dependent nuclease. MTH1203 is also shown to be a dimer and, significantly, this dimerization enhances the nuclease activity. Transcription termination in archaea produces mRNA transcripts with U-rich 3' ends that could be degraded by MTH1203 considering its RNA-binding specificity. We hypothesize that this nuclease degrades mRNAs of proteins targeted for degradation and so regulates archaeal RNA turnover, possibly in concert with the exosome.

Structure and Activity of a Novel Archaeal beta-CASP Protein with N-Terminal KH Domains.,Silva AP, Chechik M, Byrne RT, Waterman DG, Ng CL, Dodson EJ, Koonin EV, Antson AA, Smits C Structure. 2011 May 11;19(5):622-32. PMID:21565697<ref>PMID:21565697</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 2ycb" style="background-color:#fffaf0;"></div>

== References ==

<references/>

</StructureSection>

[[Category: Methanothermobacter thermautotrophicus str. Delta H]]

[[Category: Antson AA]]

[[Category: Byrne RT]]

[[Category: Chechik M]]

[[Category: Dodson EJ]]

[[Category: Koonin EV]]

[[Category: Ng CL]]

[[Category: Silva APG]]

[[Category: Smits C]]

[[Category: Waterman DG]]