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| | ==Crystal structure of ZmASCH Y47F mutant protein from Zymomonas mobilis== | | ==Crystal structure of ZmASCH Y47F mutant protein from Zymomonas mobilis== |
| - | <StructureSection load='5y6b' size='340' side='right' caption='[[5y6b]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='5y6b' size='340' side='right'caption='[[5y6b]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == 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> | + | <table><tr><td colspan='2'>[[5y6b]] is a 4 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=5Y6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5y6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y6b OCA], [https://pdbe.org/5y6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y6b RCSB], [https://www.ebi.ac.uk/pdbsum/5y6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y6b ProSAT]</span></td></tr> |
| | </table> | | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Kim, J S]] | + | [[Category: Large Structures]] |
| - | [[Category: Park, S Y]] | + | [[Category: Zymomonas mobilis subsp. mobilis ATCC 10988]] |
| - | [[Category: Rna binding protein]] | + | [[Category: Kim J-S]] |
| - | [[Category: Rna cleavage activity]] | + | [[Category: Park S-Y]] |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim BN, Shin M, Ha SC, Park SY, Seo PW, Hofmann A, Kim JS. Crystal structure of an ASCH protein from Zymomonas mobilis and its ribonuclease activity specific for single-stranded RNA. Sci Rep. 2017 Sep 26;7(1):12303. doi: 10.1038/s41598-017-12186-w. PMID:28951575 doi:http://dx.doi.org/10.1038/s41598-017-12186-w
- ↑ Kim BN, Shin M, Ha SC, Park SY, Seo PW, Hofmann A, Kim JS. Crystal structure of an ASCH protein from Zymomonas mobilis and its ribonuclease activity specific for single-stranded RNA. Sci Rep. 2017 Sep 26;7(1):12303. doi: 10.1038/s41598-017-12186-w. PMID:28951575 doi:http://dx.doi.org/10.1038/s41598-017-12186-w
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