4w8y

From Proteopedia

(Difference between revisions)

Revision as of 10:49, 4 August 2016

Structure of full length Cmr2 from Pyrococcus furiosus (Manganese bound form)

Structural highlights

4w8y is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CMR2_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. Probably not the subunit that cleaves pre-crRNA, as mutation of numerous metal-binding residues have no effect on cleavage by assembled complex.^[1]

Publication Abstract from PubMed

The Cmr complex is an RNA-guided endonuclease that cleaves foreign RNA targets as part of the CRISPR prokaryotic defense system. We investigated the molecular architecture of the P. furiosus Cmr complex using an integrative structural biology approach. We determined crystal structures of P. furiosus Cmr1, Cmr2, Cmr4, and Cmr6 and combined them with known structural information to interpret the cryo-EM map of the complex. To support structure determination, we obtained residue-specific interaction data using protein crosslinking and mass spectrometry. The resulting pseudoatomic model reveals how the superhelical backbone of the complex is defined by the polymerizing principles of Cmr4 and Cmr5 and how it is capped at the extremities by proteins of similar folds. The inner surface of the superhelix exposes conserved residues of Cmr4 that we show are required for target-cleavage activity. The structural and biochemical data thus identify Cmr4 as the conserved endoribonuclease of the Cmr complex.

Structural Model of a CRISPR RNA-Silencing Complex Reveals the RNA-Target Cleavage Activity in Cmr4.,Benda C, Ebert J, Scheltema RA, Schiller HB, Baumgartner M, Bonneau F, Mann M, Conti E Mol Cell. 2014 Oct 2;56(1):43-54. doi: 10.1016/j.molcel.2014.09.002. PMID:25280103^[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
↑ Benda C, Ebert J, Scheltema RA, Schiller HB, Baumgartner M, Bonneau F, Mann M, Conti E. Structural Model of a CRISPR RNA-Silencing Complex Reveals the RNA-Target Cleavage Activity in Cmr4. Mol Cell. 2014 Oct 2;56(1):43-54. doi: 10.1016/j.molcel.2014.09.002. PMID:25280103 doi:http://dx.doi.org/10.1016/j.molcel.2014.09.002

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/4w8y"

@@ Line 1: / Line 1: @@
 ==Structure of full length Cmr2 from Pyrococcus furiosus (Manganese bound form)==
 <StructureSection load='4w8y' size='340' side='right' caption='[[4w8y]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4w8y]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W8Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4W8Y FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4w8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w8y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4w8y RCSB], [http://www.ebi.ac.uk/pdbsum/4w8y PDBsum]</span></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=4w8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w8y OCA], [http://pdbe.org/4w8y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4w8y RCSB], [http://www.ebi.ac.uk/pdbsum/4w8y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4w8y ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4w8y" style="background-color:#fffaf0;"></div>
 ==See Also==

4w8y

From Proteopedia

Revision as of 10:49, 4 August 2016

Structure of full length Cmr2 from Pyrococcus furiosus (Manganese bound form)

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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