6ne0

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Structure of double-stranded target DNA engaged Csy complex from Pseudomonas aeruginosa (PA-14)Structure of double-stranded target DNA engaged Csy complex from Pseudomonas aeruginosa (PA-14)

Structural highlights

6ne0 is a 12 chain structure with sequence from Pseab. This structure supersedes the now removed PDB entry 6mpu. 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), cas6f, csy4, PA14_33300 (PSEAB)
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]

Publication Abstract from PubMed

Bacteria and archaea have evolved sophisticated adaptive immune systems that rely on CRISPR RNA (crRNA)-guided detection and nuclease-mediated elimination of invading nucleic acids. Here, we present the cryo-electron microscopy (cryo-EM) structure of the type I-F crRNA-guided surveillance complex (Csy complex) from Pseudomonas aeruginosa bound to a double-stranded DNA target. Comparison of this structure to previously determined structures of this complex reveals a approximately 180-degree rotation of the C-terminal helical bundle on the "large" Cas8f subunit. We show that the double-stranded DNA (dsDNA)-induced conformational change in Cas8f exposes a Cas2/3 "nuclease recruitment helix" that is structurally homologous to a virally encoded anti-CRISPR protein (AcrIF3). Structural homology between Cas8f and AcrIF3 suggests that AcrIF3 is a mimic of the Cas8f nuclease recruitment helix.

Structure Reveals a Mechanism of CRISPR-RNA-Guided Nuclease Recruitment and Anti-CRISPR Viral Mimicry.,Rollins MF, Chowdhury S, Carter J, Golden SM, Miettinen HM, Santiago-Frangos A, Faith D, Lawrence CM, Lander GC, Wiedenheft B Mol Cell. 2019 Mar 1. pii: S1097-2765(19)30091-7. doi:, 10.1016/j.molcel.2019.02.001. PMID:30872121[10]

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

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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
  7. ↑ 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
  8. ↑ 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
  9. ↑ 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
  10. ↑ Rollins MF, Chowdhury S, Carter J, Golden SM, Miettinen HM, Santiago-Frangos A, Faith D, Lawrence CM, Lander GC, Wiedenheft B. Structure Reveals a Mechanism of CRISPR-RNA-Guided Nuclease Recruitment and Anti-CRISPR Viral Mimicry. Mol Cell. 2019 Mar 1. pii: S1097-2765(19)30091-7. doi:, 10.1016/j.molcel.2019.02.001. PMID:30872121 doi:http://dx.doi.org/10.1016/j.molcel.2019.02.001

6ne0, resolution 3.40Å

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