This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4doz

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_4doz| PDB=4doz | SCENE= }}
+
==Crystal structure of Pyrococcus furiosus Cmr2 (Cas10)==
-
===Crystal structure of Pyrococcus furiosus Cmr2 (Cas10)===
+
<StructureSection load='4doz' size='340' side='right' caption='[[4doz]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
-
{{ABSTRACT_PUBMED_22449983}}
+
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[4doz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus_dsm_3638 Pyrococcus furiosus dsm 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DOZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DOZ FirstGlance]. <br>
 +
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 +
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF1129 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 Pyrococcus furiosus DSM 3638])</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=4doz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4doz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4doz RCSB], [http://www.ebi.ac.uk/pdbsum/4doz PDBsum]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
CRISPR RNAs (crRNAs) mediate sequence-specific silencing of invading viruses and plasmids in prokaryotes. The crRNA-Cmr protein complex cleaves complementary RNA. We report the crystal structure of Pyrococcus furiosus Cmr2 (Cas10), a component of this Cmr complex and the signature protein in type III CRISPR systems. The structure reveals a nucleotide cyclase domain with a set of conserved catalytic residues that associates with an unexpected deviant cyclase domain like dimeric cyclases. Additionally, two helical domains resemble the thumb domain of A-family DNA polymerase and Cmr5, respectively. Our results suggest that Cmr2 possesses novel enzymatic activity that remains to be elucidated.
-
==Function==
+
Crystal structure of Cmr2 suggests a nucleotide cyclase-related enzyme in type III CRISPR-Cas systems.,Zhu X, Ye K FEBS Lett. 2012 Mar 23;586(6):939-45. doi: 10.1016/j.febslet.2012.02.036. Epub, 2012 Feb 28. PMID:22449983<ref>PMID:22449983</ref>
-
[[http://www.uniprot.org/uniprot/CMR2_PYRFU 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.<ref>PMID:19945378</ref>
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
[[4doz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus_dsm_3638 Pyrococcus furiosus dsm 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DOZ OCA].
+
</div>
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:022449983</ref><references group="xtra"/><references/>
+
__TOC__
 +
</StructureSection>
[[Category: Pyrococcus furiosus dsm 3638]]
[[Category: Pyrococcus furiosus dsm 3638]]
-
[[Category: Ye, K.]]
+
[[Category: Ye, K]]
-
[[Category: Zhu, X.]]
+
[[Category: Zhu, X]]
[[Category: Antiviral protein]]
[[Category: Antiviral protein]]
[[Category: Crispr]]
[[Category: Crispr]]
[[Category: Cyclase]]
[[Category: Cyclase]]
[[Category: Zn]]
[[Category: Zn]]

Revision as of 09:10, 21 December 2014

Crystal structure of Pyrococcus furiosus Cmr2 (Cas10)

4doz, resolution 3.10Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4doz"
Personal tools