4wnz

From Proteopedia

(Difference between revisions)

Revision as of 13:30, 14 January 2015

Crystal structure of Pyrococcus furiosus Cmr4 (Cas7)

Structural highlights

4wnz is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[CMR4_PYRFU] 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), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation-dependent endoribonuclease activity specific for ssRNA complementary to the crRNA, generating 5' hydroxy- and 3' phosphate or 2'-3' cyclic phosphate termini. It is not known which subunit has endoribonuclease activity. Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not necessary for cleavage.^[1]

Publication Abstract from PubMed

Clustered regularly interspaced short palindromic repeat (CRISPR) loci and CRISPR-associated (Cas) proteins form an adaptive immune system that protects prokaryotes against plasmids and viruses. The Cmr complex, a type III-B effector complex, uses the CRISPR RNA (crRNA) as a guide to target RNA. Here, we show that the Cmr complex of Pyrococcus furiosus cleaves RNA at multiple sites that are 6 nt apart and are positioned relative to the 5'-end of the crRNA. We identified Cmr4 as the slicer and determined its crystal structure at 2.8 A resolution. In the crystal, Cmr4 forms a helical filament that most likely reflects its structural organization in the Cmr complex. The putative active site is located at the inner surface of the filament where the guide and substrate RNA are thought to bind. The filament structure of Cmr4 accounts for multiple periodic cleavage sites on the substrate. Our study provides new insights into the structure and mechanism of the RNA-targeting Cmr complex.

Cmr4 is the slicer in the RNA-targeting Cmr CRISPR complex.,Zhu X, Ye K Nucleic Acids Res. 2014 Dec 24. pii: gku1355. PMID:25541196^[2]

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

References

↑ Hale CR, Zhao P, Olson S, Duff MO, Graveley BR, Wells L, Terns RM, Terns MP. RNA-guided RNA cleavage by a CRISPR RNA-Cas protein complex. Cell. 2009 Nov 25;139(5):945-56. doi: 10.1016/j.cell.2009.07.040. PMID:19945378 doi:10.1016/j.cell.2009.07.040
↑ Zhu X, Ye K. Cmr4 is the slicer in the RNA-targeting Cmr CRISPR complex. Nucleic Acids Res. 2014 Dec 24. pii: gku1355. PMID:25541196 doi:http://dx.doi.org/10.1093/nar/gku1355

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4wnz"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Crystal structure of Pyrococcus furiosus Cmr4 (Cas7)==
+<StructureSection load='4wnz' size='340' side='right' caption='[[4wnz]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4wnz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WNZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WNZ FirstGlance]. <br>
+</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=4wnz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wnz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wnz RCSB], [http://www.ebi.ac.uk/pdbsum/4wnz PDBsum]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CMR4_PYRFU CMR4_PYRFU]] 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), formerly called psiRNA (prokaryotic silencing) in this organism. Part of the Cmr ribonucleoprotein complex which has divalent cation-dependent endoribonuclease activity specific for ssRNA complementary to the crRNA, generating 5' hydroxy- and 3' phosphate or 2'-3' cyclic phosphate termini. It is not known which subunit has endoribonuclease activity. Cmr complex does not cleave ssDNA complementary to the crRNA. Cleavage of invading RNA is guided by the crRNA; substrate cleavage occurs a fixed distance (14 nt) from the 3' end of the crRNA. In vitro reconstitution shows Cmr1-2 and Cmr5 are not necessary for cleavage.<ref>PMID:19945378</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Clustered regularly interspaced short palindromic repeat (CRISPR) loci and CRISPR-associated (Cas) proteins form an adaptive immune system that protects prokaryotes against plasmids and viruses. The Cmr complex, a type III-B effector complex, uses the CRISPR RNA (crRNA) as a guide to target RNA. Here, we show that the Cmr complex of Pyrococcus furiosus cleaves RNA at multiple sites that are 6 nt apart and are positioned relative to the 5'-end of the crRNA. We identified Cmr4 as the slicer and determined its crystal structure at 2.8 A resolution. In the crystal, Cmr4 forms a helical filament that most likely reflects its structural organization in the Cmr complex. The putative active site is located at the inner surface of the filament where the guide and substrate RNA are thought to bind. The filament structure of Cmr4 accounts for multiple periodic cleavage sites on the substrate. Our study provides new insights into the structure and mechanism of the RNA-targeting Cmr complex.
-The entry 4wnz is ON HOLD  until Paper Publication
+Cmr4 is the slicer in the RNA-targeting Cmr CRISPR complex.,Zhu X, Ye K Nucleic Acids Res. 2014 Dec 24. pii: gku1355. PMID:25541196<ref>PMID:25541196</ref>
-Authors: Zhu, X., Ye, K.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of Pyrococcus furiosus Cmr4 (Cas7)
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Ye, K]]
 [[Category: Zhu, X]]
+[[Category: Cmr cmplex]]
+[[Category: Crispr-cas system]]
+[[Category: Nuclease]]
+[[Category: Ramp domain]]

4wnz

From Proteopedia

Revision as of 13:30, 14 January 2015

Crystal structure of Pyrococcus furiosus Cmr4 (Cas7)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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