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| | ==Crystal structure and characterization of Cmr5 protein from Pyrococcus furiosus== | | ==Crystal structure and characterization of Cmr5 protein from Pyrococcus furiosus== |
| - | <StructureSection load='4gkf' size='340' side='right' caption='[[4gkf]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='4gkf' size='340' side='right'caption='[[4gkf]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gkf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GKF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GKF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gkf]] is a 2 chain structure with sequence from [https://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=4GKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GKF FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cmr5, PF1125 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4gkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gkf OCA], [https://pdbe.org/4gkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gkf RCSB], [https://www.ebi.ac.uk/pdbsum/4gkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gkf ProSAT]</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=4gkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gkf OCA], [http://pdbe.org/4gkf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gkf RCSB], [http://www.ebi.ac.uk/pdbsum/4gkf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gkf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CMR5_PYRFU CMR5_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. | + | [https://www.uniprot.org/uniprot/CMR5_PYRFU CMR5_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. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Endonuclease|Endonuclease]] | + | *[[Endonuclease 3D structures|Endonuclease 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pyrfu]] | + | [[Category: Large Structures]] |
| - | [[Category: Hwang, H]] | + | [[Category: Pyrococcus furiosus DSM 3638]] |
| - | [[Category: Park, J]] | + | [[Category: Hwang H]] |
| - | [[Category: Park, M]] | + | [[Category: Park J]] |
| - | [[Category: Park, S]] | + | [[Category: Park M]] |
| - | [[Category: Shin, M S]] | + | [[Category: Park S]] |
| - | [[Category: Sun, J]] | + | [[Category: Shin MS]] |
| - | [[Category: Crispr]]
| + | [[Category: Sun J]] |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
CMR5_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.
Publication Abstract from PubMed
The bacterial acquired immune system consists of clustered regularly interspaced short palindromic repeats (CRISPRs) and CRIPSR-associated (Cas) genes, which include Cas-module repeat-associated mysterious proteins (Cmr). The six Cmr proteins of Pyrococcus furiosus (pfCmr1-pfCmr6) form a Cmr effector complex that functions against exogenous nucleic acid. Among the Cmr proteins, the role of pfCmr5 and its involvement in the complex's cleavage activity have been obscure. The elucidated pfCmr5 structure has two inserted alpha-helices compared with the other trimeric Cmr5 structure. However, pfCmr5 exists as a monomeric protein both in the crystalline state and in solution. In vitro assays indicate that pfCmr5 interacts with pfCmr4. These structural and biophysical data might help in understanding the complicated and ill-characterized Cmr effector complex.
Crystal structure of Cmr5 from Pyrococcus furiosus and its functional implications.,Park JH, Sun J, Park SY, Hwang HJ, Park MY, Shin M, Kim JS FEBS Lett. 2013 Mar 18;587(6):562-8. doi: 10.1016/j.febslet.2013.01.029. Epub, 2013 Jan 28. PMID:23370277[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Park JH, Sun J, Park SY, Hwang HJ, Park MY, Shin M, Kim JS. Crystal structure of Cmr5 from Pyrococcus furiosus and its functional implications. FEBS Lett. 2013 Mar 18;587(6):562-8. doi: 10.1016/j.febslet.2013.01.029. Epub, 2013 Jan 28. PMID:23370277 doi:10.1016/j.febslet.2013.01.029
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