5y6b: Difference between revisions
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==Crystal structure of ZmASCH Y47F mutant protein from Zymomonas mobilis== | |||
<StructureSection load='5y6b' size='340' side='right' caption='[[5y6b]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5y6b]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y6B FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5guq|5guq]], [[5gus|5gus]]</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=5y6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y6b OCA], [http://pdbe.org/5y6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y6b RCSB], [http://www.ebi.ac.uk/pdbsum/5y6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y6b ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Activating signal cointegrator-1 homology (ASCH) domains were initially reported in human as a part of the ASC-1 transcriptional regulator, a component of a putative RNA-interacting protein complex; their presence has now been confirmed in a wide range of organisms. Here, we have determined the trigonal and monoclinic crystal structures of an ASCH domain-containing protein from Zymomonas mobilis (ZmASCH), and analyzed the structural determinants of its nucleic acid processing activity. The protein has a central beta-barrel structure with several nearby alpha-helices. Positively charged surface patches form a cleft that runs through the pocket formed between the beta-barrel and the surrounding alpha-helices. We further demonstrate by means of in vitro assays that ZmASCH binds nucleic acids, and degrades single-stranded RNAs in a magnesium ion-dependent manner with a cleavage preference for the phosphodiester bond between the pyrimidine and adenine nucleotides. ZmASCH also removes a nucleotide at the 5'-end. Mutagenesis studies, guided by molecular dynamics simulations, confirmed that three residues (Tyr47, Lys53, and Ser128) situated in the cleft contribute to nucleic acid-binding and RNA cleavage activities. These structural and biochemical studies imply that prokaryotic ASCH may function to control the cellular RNA amount. | |||
Crystal structure of an ASCH protein from Zymomonas mobilis and its ribonuclease activity specific for single-stranded RNA.,Kim BN, Shin M, Ha SC, Park SY, Seo PW, Hofmann A, Kim JS Sci Rep. 2017 Sep 26;7(1):12303. doi: 10.1038/s41598-017-12186-w. PMID:28951575<ref>PMID:28951575</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5y6b" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kim, J S]] | |||
[[Category: Park, S Y]] | |||
[[Category: Rna binding protein]] | |||
[[Category: Rna cleavage activity]] | |||
Revision as of 07:30, 18 July 2018
Crystal structure of ZmASCH Y47F mutant protein from Zymomonas mobilis
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