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5uz9

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Revision as of 22:00, 10 April 2020

Cryo EM structure of anti-CRISPRs, AcrF1 and AcrF2, bound to type I-F crRNA-guided CRISPR surveillance complex

5uz9, resolution 3.40Å

Structural highlights

5uz9 is a 13 chain structure with sequence from Bpd31, Pseab and Pseudomonas phage jbd30. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	csy1, PA14_33330 (PSEAB), csy2, PA14_33320 (PSEAB), csy3, csy1-3, PA14_33310 (PSEAB), JBD30_035 (Pseudomonas phage JBD30), orf30 (BPD31), cas6f, csy4, PA14_33300 (PSEAB)
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] ^[3] [CSY1_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.^[4] ^[5] [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.^[6] ^[7] [CSY2_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). Absolutely required for crRNA production or stability. The Csy ribonucleoprotein complex binds target ssDNA with high affinity but target dsDNA with much lower affinity.^[8] ^[9] [ACR30_BPD31] Allows the phage to evade the CRISPR/Cas system type I-F.^[10]

Publication Abstract from PubMed

Genetic conflict between viruses and their hosts drives evolution and genetic innovation. Prokaryotes evolved CRISPR-mediated adaptive immune systems for protection from viral infection, and viruses have evolved diverse anti-CRISPR (Acr) proteins that subvert these immune systems. The adaptive immune system in Pseudomonas aeruginosa (type I-F) relies on a 350 kDa CRISPR RNA (crRNA)-guided surveillance complex (Csy complex) to bind foreign DNA and recruit a trans-acting nuclease for target degradation. Here, we report the cryo-electron microscopy (cryo-EM) structure of the Csy complex bound to two different Acr proteins, AcrF1 and AcrF2, at an average resolution of 3.4 A. The structure explains the molecular mechanism for immune system suppression, and structure-guided mutations show that the Acr proteins bind to residues essential for crRNA-mediated detection of DNA. Collectively, these data provide a snapshot of an ongoing molecular arms race between viral suppressors and the immune system they target.

Structure Reveals Mechanisms of Viral Suppressors that Intercept a CRISPR RNA-Guided Surveillance Complex.,Chowdhury S, Carter J, Rollins MF, Golden SM, Jackson RN, Hoffmann C, Nosaka L, Bondy-Denomy J, Maxwell KL, Davidson AR, Fischer ER, Lander GC, Wiedenheft B Cell. 2017 Mar 23;169(1):47-57.e11. doi: 10.1016/j.cell.2017.03.012. PMID:28340349^[11]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Haurwitz RE, Jinek M, Wiedenheft B, Zhou K, Doudna JA. Sequence- and structure-specific RNA processing by a CRISPR endonuclease. Science. 2010 Sep 10;329(5997):1355-8. PMID:20829488 doi:10.1126/science.1192272
↑ Cady KC, O'Toole GA. Non-identity-mediated CRISPR-bacteriophage interaction mediated via the Csy and Cas3 proteins. J Bacteriol. 2011 Jul;193(14):3433-45. doi: 10.1128/JB.01411-10. Epub 2011 Mar, 11. PMID:21398535 doi:http://dx.doi.org/10.1128/JB.01411-10
↑ Haurwitz RE, Sternberg SH, Doudna JA. Csy4 relies on an unusual catalytic dyad to position and cleave CRISPR RNA. EMBO J. 2012 Apr 20. doi: 10.1038/emboj.2012.107. PMID:22522703 doi:10.1038/emboj.2012.107
↑ Cady KC, O'Toole GA. Non-identity-mediated CRISPR-bacteriophage interaction mediated via the Csy and Cas3 proteins. J Bacteriol. 2011 Jul;193(14):3433-45. doi: 10.1128/JB.01411-10. Epub 2011 Mar, 11. PMID:21398535 doi:http://dx.doi.org/10.1128/JB.01411-10
↑ Haurwitz RE, Sternberg SH, Doudna JA. Csy4 relies on an unusual catalytic dyad to position and cleave CRISPR RNA. EMBO J. 2012 Apr 20. doi: 10.1038/emboj.2012.107. PMID:22522703 doi:10.1038/emboj.2012.107
↑ Cady KC, O'Toole GA. Non-identity-mediated CRISPR-bacteriophage interaction mediated via the Csy and Cas3 proteins. J Bacteriol. 2011 Jul;193(14):3433-45. doi: 10.1128/JB.01411-10. Epub 2011 Mar, 11. PMID:21398535 doi:http://dx.doi.org/10.1128/JB.01411-10
↑ Haurwitz RE, Sternberg SH, Doudna JA. Csy4 relies on an unusual catalytic dyad to position and cleave CRISPR RNA. EMBO J. 2012 Apr 20. doi: 10.1038/emboj.2012.107. PMID:22522703 doi:10.1038/emboj.2012.107
↑ Cady KC, O'Toole GA. Non-identity-mediated CRISPR-bacteriophage interaction mediated via the Csy and Cas3 proteins. J Bacteriol. 2011 Jul;193(14):3433-45. doi: 10.1128/JB.01411-10. Epub 2011 Mar, 11. PMID:21398535 doi:http://dx.doi.org/10.1128/JB.01411-10
↑ Haurwitz RE, Sternberg SH, Doudna JA. Csy4 relies on an unusual catalytic dyad to position and cleave CRISPR RNA. EMBO J. 2012 Apr 20. doi: 10.1038/emboj.2012.107. PMID:22522703 doi:10.1038/emboj.2012.107
↑ Bondy-Denomy J, Pawluk A, Maxwell KL, Davidson AR. Bacteriophage genes that inactivate the CRISPR/Cas bacterial immune system. Nature. 2013 Jan 17;493(7432):429-32. doi: 10.1038/nature11723. Epub 2012 Dec 16. PMID:23242138 doi:http://dx.doi.org/10.1038/nature11723
↑ Chowdhury S, Carter J, Rollins MF, Golden SM, Jackson RN, Hoffmann C, Nosaka L, Bondy-Denomy J, Maxwell KL, Davidson AR, Fischer ER, Lander GC, Wiedenheft B. Structure Reveals Mechanisms of Viral Suppressors that Intercept a CRISPR RNA-Guided Surveillance Complex. Cell. 2017 Mar 23;169(1):47-57.e11. doi: 10.1016/j.cell.2017.03.012. PMID:28340349 doi:http://dx.doi.org/10.1016/j.cell.2017.03.012

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5uz9"

@@ Line 3: / Line 3: @@
 <SX load='5uz9' size='340' side='right' viewer='molstar' caption='[[5uz9]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5uz9]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpd31 Bpd31], [http://en.wikipedia.org/wiki/Pseab Pseab] and [http://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=5UZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5UZ9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5uz9]] is a 13 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpd31 Bpd31], [http://en.wikipedia.org/wiki/Pseab Pseab] and [http://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=5UZ9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UZ9 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">csy1, PA14_33330 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208963 PSEAB]), csy2, PA14_33320 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208963 PSEAB]), csy3, csy1-3, PA14_33310 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208963 PSEAB]), JBD30_035 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1223260 Pseudomonas phage JBD30]), orf30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10708 BPD31]), cas6f, csy4, PA14_33300 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208963 PSEAB])</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=5uz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uz9 OCA], [http://pdbe.org/5uz9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uz9 RCSB], [http://www.ebi.ac.uk/pdbsum/5uz9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uz9 ProSAT]</span></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=5uz9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5uz9 OCA], [http://pdbe.org/5uz9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5uz9 RCSB], [http://www.ebi.ac.uk/pdbsum/5uz9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5uz9 ProSAT]</span></td></tr>
 </table>
 == Function ==

5uz9

From Proteopedia

Revision as of 22:00, 10 April 2020

Cryo EM structure of anti-CRISPRs, AcrF1 and AcrF2, bound to type I-F crRNA-guided CRISPR surveillance complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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