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| | ==Crystal structure of ASCH from Zymomonas mobilis== | | ==Crystal structure of ASCH from Zymomonas mobilis== |
| - | <StructureSection load='5guq' size='340' side='right' caption='[[5guq]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='5guq' size='340' side='right'caption='[[5guq]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5guq]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Zymma Zymma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GUQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GUQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5guq]] 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=5GUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GUQ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[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]] 1.697Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Zmob_0380 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=555217 ZYMMA])</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=5guq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5guq OCA], [https://pdbe.org/5guq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5guq RCSB], [https://www.ebi.ac.uk/pdbsum/5guq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5guq ProSAT]</span></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=5guq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5guq OCA], [http://pdbe.org/5guq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5guq RCSB], [http://www.ebi.ac.uk/pdbsum/5guq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5guq ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [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> |
| - | 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.
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| - | 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>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 5guq" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Zymma]] | + | [[Category: Large Structures]] |
| - | [[Category: Ha, S C]] | + | [[Category: Zymomonas mobilis subsp. mobilis ATCC 10988]] |
| - | [[Category: Kim, J S]] | + | [[Category: Ha SC]] |
| - | [[Category: Park, S Y]] | + | [[Category: Kim JS]] |
| - | [[Category: Hydrolase]] | + | [[Category: Park SY]] |
| - | [[Category: Nuclease]]
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