6b46: Difference between revisions

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<SX load='6b46' size='340' side='right' viewer='molstar' caption='[[6b46]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<SX load='6b46' size='340' side='right' viewer='molstar' caption='[[6b46]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6b46]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B46 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6B46 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6b46]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa], [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_UCBPP-PA14 Pseudomonas aeruginosa UCBPP-PA14] and [https://en.wikipedia.org/wiki/Pseudomonas_phage_JBD30 Pseudomonas phage JBD30]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B46 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6b44|6b44]], [[6b45|6b45]], [[6b47|6b47]], [[6b48|6b48]]</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]] 3.1&#8491;</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=6b46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b46 OCA], [http://pdbe.org/6b46 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b46 RCSB], [http://www.ebi.ac.uk/pdbsum/6b46 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b46 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=6b46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b46 OCA], [https://pdbe.org/6b46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b46 RCSB], [https://www.ebi.ac.uk/pdbsum/6b46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b46 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CSY3_PSEAB CSY3_PSEAB]] CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 and Cascade participate in CRISPR interference, the third stage of CRISPR immunity (Potential). Involved in crRNA production or stability. The Csy ribonucleoprotein complex binds target ssDNA with high affinity but target dsDNA with much lower affinity.<ref>PMID:21398535</ref> <ref>PMID:22522703</ref>  [[http://www.uniprot.org/uniprot/CAS6_PSEAB CAS6_PSEAB]] CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Processes pre-crRNA into individual crRNA units. Absolutely required for crRNA production or stability. Upon expression in E.coli endonucleolytically processes pre-crRNA, although disruption and reconstitution experiments indicate that in situ other genes are also required for processing. Yields 5'-hydroxy and 3'-phosphate groups. The Csy ribonucleoprotein complex binds target ssDNA with high affinity but target dsDNA with much lower affinity.<ref>PMID:20829488</ref> <ref>PMID:21398535</ref> <ref>PMID:22522703</ref> 
[https://www.uniprot.org/uniprot/CSY3_PSEAB CSY3_PSEAB] CRISPR (clustered regularly interspaced short palindromic repeat) is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Cas3 and Cascade participate in CRISPR interference, the third stage of CRISPR immunity (Potential). Involved in crRNA production or stability. The Csy ribonucleoprotein complex binds target ssDNA with high affinity but target dsDNA with much lower affinity.<ref>PMID:21398535</ref> <ref>PMID:22522703</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Prokaryotic cells possess CRISPR-mediated adaptive immune systems that protect them from foreign genetic elements, such as invading viruses. A central element of this immune system is an RNA-guided surveillance complex capable of targeting non-self DNA or RNA for degradation in a sequence- and site-specific manner analogous to RNA interference. Although the complexes display considerable diversity in their composition and architecture, many basic mechanisms underlying target recognition and cleavage are highly conserved. Using cryoelectron microscopy (cryo-EM), we show that the binding of target double-stranded DNA (dsDNA) to a type I-F CRISPR system yersinia (Csy) surveillance complex leads to large quaternary and tertiary structural changes in the complex that are likely necessary in the pathway leading to target dsDNA degradation by a trans-acting helicase-nuclease. Comparison of the structure of the surveillance complex before and after dsDNA binding, or in complex with three virally encoded anti-CRISPR suppressors that inhibit dsDNA binding, reveals mechanistic details underlying target recognition and inhibition.
 
Cryo-EM Structures Reveal Mechanism and Inhibition of DNA Targeting by a CRISPR-Cas Surveillance Complex.,Guo TW, Bartesaghi A, Yang H, Falconieri V, Rao P, Merk A, Eng ET, Raczkowski AM, Fox T, Earl LA, Patel DJ, Subramaniam S Cell. 2017 Oct 5;171(2):414-426.e12. doi: 10.1016/j.cell.2017.09.006. PMID:28985564<ref>PMID:28985564</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6b46" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bartesaghi, A]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Earl, L]]
[[Category: Pseudomonas aeruginosa UCBPP-PA14]]
[[Category: Falconieri, V]]
[[Category: Pseudomonas phage JBD30]]
[[Category: Fox, T]]
[[Category: Bartesaghi A]]
[[Category: Guo, T W]]
[[Category: Earl L]]
[[Category: Merk, A]]
[[Category: Falconieri V]]
[[Category: Patel, D J]]
[[Category: Fox T]]
[[Category: Rao, P]]
[[Category: Guo TW]]
[[Category: Subramaniam, S]]
[[Category: Merk A]]
[[Category: Yang, H]]
[[Category: Patel DJ]]
[[Category: Crispr-ca]]
[[Category: Rao P]]
[[Category: Immune system-hydrolase-rna complex]]
[[Category: Subramaniam S]]
[[Category: Yang H]]

Latest revision as of 17:20, 13 March 2024

Cryo-EM structure of Type I-F CRISPR crRNA-guided Csy surveillance complex with bound anti-CRISPR protein AcrF1Cryo-EM structure of Type I-F CRISPR crRNA-guided Csy surveillance complex with bound anti-CRISPR protein AcrF1

6b46, resolution 3.10Å

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