5y6c: Difference between revisions
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==Crystal structure of ZmASCH S128A mutant protein from Zymomonas mobilis== | |||
<StructureSection load='5y6c' size='340' side='right'caption='[[5y6c]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5y6c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zymomonas_mobilis_subsp._mobilis_ATCC_10988 Zymomonas mobilis subsp. mobilis ATCC 10988]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y6C 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]] 2.398Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5y6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y6c OCA], [https://pdbe.org/5y6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y6c RCSB], [https://www.ebi.ac.uk/pdbsum/5y6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y6c ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ASCHD_ZYMMA ASCHD_ZYMMA] Shows sequence-specific endoribonuclease activity towards single-stranded RNA (ssRNA), with a preference for the bond between pyrimidine and adenine nucleotides. May also have 5'-exonuclease activity.<ref>PMID:28951575</ref> | |||
<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> | ||
[[Category: | <div class="pdbe-citations 5y6c" style="background-color:#fffaf0;"></div> | ||
[[Category: Kim | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Zymomonas mobilis subsp. mobilis ATCC 10988]] | |||
[[Category: Kim J-S]] | |||
[[Category: Park S-Y]] | |||