6s8b: Difference between revisions
m Protected "6s8b" [edit=sysop:move=sysop] |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Cryo-EM structure of the Type III-B Cmr-beta bound to cognate target RNA and AMPPnP, state 1== | |||
<StructureSection load='6s8b' size='340' side='right'caption='[[6s8b]], [[Resolution|resolution]] 2.41Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6s8b]] is a 35 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulir Sulir], [http://en.wikipedia.org/wiki/Sulfolobus_islandicus_(strain_rey15a) Sulfolobus islandicus (strain rey15a)] and [http://en.wikipedia.org/wiki/Sulfolobus_islandicus_rey15a Sulfolobus islandicus rey15a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S8B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6S8B FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SiRe_0599 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=930945 SULIR])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6s8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s8b OCA], [http://pdbe.org/6s8b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s8b RCSB], [http://www.ebi.ac.uk/pdbsum/6s8b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s8b ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cmr-beta is a type III-B CRISPR-Cas complex that, upon target RNA recognition, unleashes a multifaceted immune response against invading genetic elements, including single-stranded DNA (ssDNA) cleavage, cyclic oligoadenylate synthesis, and also a unique UA-specific single-stranded RNA (ssRNA) hydrolysis by the Cmr2 subunit. Here, we present the structure-function relationship of Cmr-beta, unveiling how binding of the target RNA regulates the Cmr2 activities. Cryoelectron microscopy (cryo-EM) analysis revealed the unique subunit architecture of Cmr-beta and captured the complex in different conformational stages of the immune response, including the non-cognate and cognate target-RNA-bound complexes. The binding of the target RNA induces a conformational change of Cmr2, which together with the complementation between the 5' tag in the CRISPR RNAs (crRNA) and the 3' antitag of the target RNA activate different configurations in a unique loop of the Cmr3 subunit, which acts as an allosteric sensor signaling the self- versus non-self-recognition. These findings highlight the diverse defense strategies of type III complexes. | |||
Structures of the Cmr-beta Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas.,Sofos N, Feng M, Stella S, Pape T, Fuglsang A, Lin J, Huang Q, Li Y, She Q, Montoya G Mol Cell. 2020 Jul 29. pii: S1097-2765(20)30474-3. doi:, 10.1016/j.molcel.2020.07.008. PMID:32730741<ref>PMID:32730741</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6s8b" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sulfolobus islandicus rey15a]] | |||
[[Category: Sulir]] | |||
[[Category: Montoya, G]] | |||
[[Category: Sofos, N]] | |||
[[Category: Stella, S]] | |||
[[Category: Antiviral protein]] | |||
[[Category: Crispr-ca]] | |||
[[Category: Cyclic oligo-adenylate synthase]] | |||
[[Category: Effector complex]] | |||
[[Category: Nuclease]] | |||
Latest revision as of 12:59, 12 August 2020
Cryo-EM structure of the Type III-B Cmr-beta bound to cognate target RNA and AMPPnP, state 1Cryo-EM structure of the Type III-B Cmr-beta bound to cognate target RNA and AMPPnP, state 1
Structural highlights
Publication Abstract from PubMedCmr-beta is a type III-B CRISPR-Cas complex that, upon target RNA recognition, unleashes a multifaceted immune response against invading genetic elements, including single-stranded DNA (ssDNA) cleavage, cyclic oligoadenylate synthesis, and also a unique UA-specific single-stranded RNA (ssRNA) hydrolysis by the Cmr2 subunit. Here, we present the structure-function relationship of Cmr-beta, unveiling how binding of the target RNA regulates the Cmr2 activities. Cryoelectron microscopy (cryo-EM) analysis revealed the unique subunit architecture of Cmr-beta and captured the complex in different conformational stages of the immune response, including the non-cognate and cognate target-RNA-bound complexes. The binding of the target RNA induces a conformational change of Cmr2, which together with the complementation between the 5' tag in the CRISPR RNAs (crRNA) and the 3' antitag of the target RNA activate different configurations in a unique loop of the Cmr3 subunit, which acts as an allosteric sensor signaling the self- versus non-self-recognition. These findings highlight the diverse defense strategies of type III complexes. Structures of the Cmr-beta Complex Reveal the Regulation of the Immunity Mechanism of Type III-B CRISPR-Cas.,Sofos N, Feng M, Stella S, Pape T, Fuglsang A, Lin J, Huang Q, Li Y, She Q, Montoya G Mol Cell. 2020 Jul 29. pii: S1097-2765(20)30474-3. doi:, 10.1016/j.molcel.2020.07.008. PMID:32730741[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||