7uzy
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7uzy]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_epidermidis_RP62A Staphylococcus epidermidis RP62A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UZY FirstGlance]. <br> | <table><tr><td colspan='2'>[[7uzy]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_epidermidis_RP62A Staphylococcus epidermidis RP62A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7UZY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7UZY FirstGlance]. <br> | ||
| - | </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=7uzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uzy OCA], [https://pdbe.org/7uzy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uzy RCSB], [https://www.ebi.ac.uk/pdbsum/7uzy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uzy ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.05Å</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=7uzy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7uzy OCA], [https://pdbe.org/7uzy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7uzy RCSB], [https://www.ebi.ac.uk/pdbsum/7uzy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7uzy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/Q5HK89_STAEQ Q5HK89_STAEQ] | |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Clustered regularly interspaced short palindromic repeats (CRISPR) and their CRISPR-associated proteins (Cas) provide many prokaryotes with an adaptive immune system against invading genetic material. Type III CRISPR systems are unique in that they can degrade both RNA and DNA. In response to invading nucleic acids, they produce cyclic oligoadenylates that act as secondary messengers, activating cellular nucleases that aid in the immune response. Here, we present seven single-particle cryo-EM structures of the type III-A Staphylococcus epidermidis CRISPR effector complex. The structures reveal the intact S. epidermidis effector complex in an apo, ATP-bound, cognate target RNA-bound, and non-cognate target RNA-bound states and illustrate how the effector complex binds and presents crRNA. The complexes bound to target RNA capture the type III-A effector complex in a post-RNA cleavage state. The ATP-bound structures give details about how ATP binds to Cas10 to facilitate cyclic oligoadenylate production. | Clustered regularly interspaced short palindromic repeats (CRISPR) and their CRISPR-associated proteins (Cas) provide many prokaryotes with an adaptive immune system against invading genetic material. Type III CRISPR systems are unique in that they can degrade both RNA and DNA. In response to invading nucleic acids, they produce cyclic oligoadenylates that act as secondary messengers, activating cellular nucleases that aid in the immune response. Here, we present seven single-particle cryo-EM structures of the type III-A Staphylococcus epidermidis CRISPR effector complex. The structures reveal the intact S. epidermidis effector complex in an apo, ATP-bound, cognate target RNA-bound, and non-cognate target RNA-bound states and illustrate how the effector complex binds and presents crRNA. The complexes bound to target RNA capture the type III-A effector complex in a post-RNA cleavage state. The ATP-bound structures give details about how ATP binds to Cas10 to facilitate cyclic oligoadenylate production. | ||
| - | Structures of an active type III-A CRISPR effector complex.,Smith EM, Ferrell S, Tokars VL, Mondragon A Structure. 2022 Aug 4;30(8):1109-1128.e6. doi: 10.1016/j.str.2022.05.013. Epub, 2022 Jun 16. PMID:35714601<ref>PMID:35714601</ref> | + | Structures of an active type III-A CRISPR effector complex.,Smith EM, Ferrell S, Tokars VL, Mondragon A Structure. 2022 Aug 4;30(8):1109-1128.e6. doi: 10.1016/j.str.2022.05.013. Epub , 2022 Jun 16. PMID:35714601<ref>PMID:35714601</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
Current revision
Staphylococcus epidermidis RP62A CRISPR effector complex with non-self target RNA 2
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