Crystal structure and CRISPR RNA-binding site of the Cmr1 subunit of the Cmr interference complex
A multi‐subunit ribonucleoprotein complex termed the Cmr RNA‐silencing complex recognizes and destroys viral RNA in the CRISPR‐mediated immune defence mechanism in many prokaryotes using an as yet unclear mechanism. In Archaeoglobus fulgidus, this complex consists of six subunits, Cmr1–Cmr6. Here, t...
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2014-02, Vol.70 (2), p.535-543 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
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| creator | Sun, Jiali Jeon, Jae-Hyun Shin, Minsang Shin, Ho-Chul Oh, Byung-Ha Kim, Jeong-Sun |
| description | A multi‐subunit ribonucleoprotein complex termed the Cmr RNA‐silencing complex recognizes and destroys viral RNA in the CRISPR‐mediated immune defence mechanism in many prokaryotes using an as yet unclear mechanism. In Archaeoglobus fulgidus, this complex consists of six subunits, Cmr1–Cmr6. Here, the crystal structure of Cmr1 from A. fulgidus is reported, revealing that the protein is composed of two tightly associated ferredoxin‐like domains. The domain located at the N‐terminus is structurally most similar to the N‐terminal ferredoxin‐like domain of the CRISPR RNA‐processing enzyme Cas6 from Pyrococcus furiosus. An ensuing mutational analysis identified a highly conserved basic surface patch that binds single‐stranded nucleic acids specifically, including the mature CRISPR RNA, but in a sequence‐independent manner. In addition, this subunit was found to cleave single‐stranded RNA. Together, these studies elucidate the structure and the catalytic activity of the Cmr1 subunit. |
| doi_str_mv | 10.1107/S1399004713030290 |
| format | Article |
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In Archaeoglobus fulgidus, this complex consists of six subunits, Cmr1–Cmr6. Here, the crystal structure of Cmr1 from A. fulgidus is reported, revealing that the protein is composed of two tightly associated ferredoxin‐like domains. The domain located at the N‐terminus is structurally most similar to the N‐terminal ferredoxin‐like domain of the CRISPR RNA‐processing enzyme Cas6 from Pyrococcus furiosus. An ensuing mutational analysis identified a highly conserved basic surface patch that binds single‐stranded nucleic acids specifically, including the mature CRISPR RNA, but in a sequence‐independent manner. In addition, this subunit was found to cleave single‐stranded RNA. Together, these studies elucidate the structure and the catalytic activity of the Cmr1 subunit.</description><identifier>ISSN: 1399-0047</identifier><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><identifier>DOI: 10.1107/S1399004713030290</identifier><identifier>PMID: 24531487</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Amino Acid Sequence ; Archaeal Proteins - chemistry ; Archaeal Proteins - genetics ; Archaeal Proteins - metabolism ; Archaeoglobus fulgidus ; Archaeoglobus fulgidus - chemistry ; Archaeoglobus fulgidus - immunology ; Archaeoglobus fulgidus - virology ; Bacteriology ; Binding Sites ; Clustered Regularly Interspaced Short Palindromic Repeats - genetics ; Clustered Regularly Interspaced Short Palindromic Repeats - immunology ; Cmr interference complex ; Cmr1 subunit ; Crystal structure ; Crystallography, X-Ray ; Escherichia coli - genetics ; Escherichia coli - metabolism ; Ferredoxins - chemistry ; Ferredoxins - genetics ; Ferredoxins - metabolism ; Host-Pathogen Interactions ; Models, Molecular ; Molecular Sequence Data ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits - chemistry ; Protein Subunits - genetics ; Protein Subunits - metabolism ; Pyrococcus furiosus - chemistry ; Pyrococcus furiosus - genetics ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; RNA, Viral - chemistry ; RNA, Viral - metabolism ; RNA-binding site ; Sequence Alignment ; Structural Homology, Protein ; Substrate Specificity</subject><ispartof>Acta crystallographica. 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Section D, Biological crystallography.</title><addtitle>Acta Crystallographica D</addtitle><description>A multi‐subunit ribonucleoprotein complex termed the Cmr RNA‐silencing complex recognizes and destroys viral RNA in the CRISPR‐mediated immune defence mechanism in many prokaryotes using an as yet unclear mechanism. In Archaeoglobus fulgidus, this complex consists of six subunits, Cmr1–Cmr6. Here, the crystal structure of Cmr1 from A. fulgidus is reported, revealing that the protein is composed of two tightly associated ferredoxin‐like domains. The domain located at the N‐terminus is structurally most similar to the N‐terminal ferredoxin‐like domain of the CRISPR RNA‐processing enzyme Cas6 from Pyrococcus furiosus. An ensuing mutational analysis identified a highly conserved basic surface patch that binds single‐stranded nucleic acids specifically, including the mature CRISPR RNA, but in a sequence‐independent manner. In addition, this subunit was found to cleave single‐stranded RNA. Together, these studies elucidate the structure and the catalytic activity of the Cmr1 subunit.</description><subject>Amino Acid Sequence</subject><subject>Archaeal Proteins - chemistry</subject><subject>Archaeal Proteins - genetics</subject><subject>Archaeal Proteins - metabolism</subject><subject>Archaeoglobus fulgidus</subject><subject>Archaeoglobus fulgidus - chemistry</subject><subject>Archaeoglobus fulgidus - immunology</subject><subject>Archaeoglobus fulgidus - virology</subject><subject>Bacteriology</subject><subject>Binding Sites</subject><subject>Clustered Regularly Interspaced Short Palindromic Repeats - genetics</subject><subject>Clustered Regularly Interspaced Short Palindromic Repeats - immunology</subject><subject>Cmr interference complex</subject><subject>Cmr1 subunit</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Escherichia coli - genetics</subject><subject>Escherichia coli - metabolism</subject><subject>Ferredoxins - chemistry</subject><subject>Ferredoxins - genetics</subject><subject>Ferredoxins - metabolism</subject><subject>Host-Pathogen Interactions</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Protein Structure, Secondary</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - genetics</subject><subject>Protein Subunits - metabolism</subject><subject>Pyrococcus furiosus - chemistry</subject><subject>Pyrococcus furiosus - genetics</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>RNA, Viral - chemistry</subject><subject>RNA, Viral - metabolism</subject><subject>RNA-binding site</subject><subject>Sequence Alignment</subject><subject>Structural Homology, Protein</subject><subject>Substrate Specificity</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtP3DAUha2qVXm0P6CbylI33aRcPxInyyEUioQADVSoK8t2blrTPKa2ozL_nowGEGoXrGwdfd-RdUzIBwZfGAN1cMVEVQFIxQQI4BW8IrubKNtkr5_dd8hejLcAwLlQb8kOl7lgslS7xNRhHZPpaExhcmkKSM3Q0Hp5enW5pMvzRWb90PjhJ40-IR1bmn4hrfvAaJzsNPj0LKN-SBhaDDg4pG7sVx3evSNvWtNFfP9w7pPvx1-v62_Z2cXJab04y5wshciQ25wxVnDJHSsa6ZxiZcNc2yphG2GlRTS5zVGWRSFKwUtQJVauagCMhULsk8_b3lUY_0wYk-59dNh1ZsBxiprlAApEDmpGP_2D3o5TGObXaSarUkouJcwU21IujDEGbPUq-N6EtWagN_vr__afnY8PzZPtsXkyHgefgWoL_PUdrl9u1IsfR_zmKJ8_bnazretjwrsn14TfulBC5frm_ERfX8Lh4fJY6ELcA7TXnPc</recordid><startdate>201402</startdate><enddate>201402</enddate><creator>Sun, Jiali</creator><creator>Jeon, Jae-Hyun</creator><creator>Shin, Minsang</creator><creator>Shin, Ho-Chul</creator><creator>Oh, Byung-Ha</creator><creator>Kim, Jeong-Sun</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, Inc</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7SP</scope><scope>7SR</scope><scope>7TK</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>H8D</scope><scope>JG9</scope><scope>L7M</scope><scope>7X8</scope></search><sort><creationdate>201402</creationdate><title>Crystal structure and CRISPR RNA-binding site of the Cmr1 subunit of the Cmr interference complex</title><author>Sun, Jiali ; Jeon, Jae-Hyun ; Shin, Minsang ; Shin, Ho-Chul ; Oh, Byung-Ha ; Kim, Jeong-Sun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4833-e2b51116242c16d4cc718d1cff73bd3b4beea5b5e486638328078e9c9d00ab063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>Archaeal Proteins - chemistry</topic><topic>Archaeal Proteins - genetics</topic><topic>Archaeal Proteins - metabolism</topic><topic>Archaeoglobus fulgidus</topic><topic>Archaeoglobus fulgidus - chemistry</topic><topic>Archaeoglobus fulgidus - immunology</topic><topic>Archaeoglobus fulgidus - virology</topic><topic>Bacteriology</topic><topic>Binding Sites</topic><topic>Clustered Regularly Interspaced Short Palindromic Repeats - genetics</topic><topic>Clustered Regularly Interspaced Short Palindromic Repeats - immunology</topic><topic>Cmr interference complex</topic><topic>Cmr1 subunit</topic><topic>Crystal structure</topic><topic>Crystallography, X-Ray</topic><topic>Escherichia coli - genetics</topic><topic>Escherichia coli - metabolism</topic><topic>Ferredoxins - chemistry</topic><topic>Ferredoxins - genetics</topic><topic>Ferredoxins - metabolism</topic><topic>Host-Pathogen Interactions</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Protein Structure, Secondary</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Subunits - chemistry</topic><topic>Protein Subunits - genetics</topic><topic>Protein Subunits - metabolism</topic><topic>Pyrococcus furiosus - chemistry</topic><topic>Pyrococcus furiosus - genetics</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>RNA, Viral - chemistry</topic><topic>RNA, Viral - metabolism</topic><topic>RNA-binding site</topic><topic>Sequence Alignment</topic><topic>Structural Homology, Protein</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sun, Jiali</creatorcontrib><creatorcontrib>Jeon, Jae-Hyun</creatorcontrib><creatorcontrib>Shin, Minsang</creatorcontrib><creatorcontrib>Shin, Ho-Chul</creatorcontrib><creatorcontrib>Oh, Byung-Ha</creatorcontrib><creatorcontrib>Kim, Jeong-Sun</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Aerospace Database</collection><collection>Materials Research Database</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Acta crystallographica. 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Section D, Biological crystallography.</jtitle><addtitle>Acta Crystallographica D</addtitle><date>2014-02</date><risdate>2014</risdate><volume>70</volume><issue>2</issue><spage>535</spage><epage>543</epage><pages>535-543</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>A multi‐subunit ribonucleoprotein complex termed the Cmr RNA‐silencing complex recognizes and destroys viral RNA in the CRISPR‐mediated immune defence mechanism in many prokaryotes using an as yet unclear mechanism. In Archaeoglobus fulgidus, this complex consists of six subunits, Cmr1–Cmr6. Here, the crystal structure of Cmr1 from A. fulgidus is reported, revealing that the protein is composed of two tightly associated ferredoxin‐like domains. The domain located at the N‐terminus is structurally most similar to the N‐terminal ferredoxin‐like domain of the CRISPR RNA‐processing enzyme Cas6 from Pyrococcus furiosus. An ensuing mutational analysis identified a highly conserved basic surface patch that binds single‐stranded nucleic acids specifically, including the mature CRISPR RNA, but in a sequence‐independent manner. In addition, this subunit was found to cleave single‐stranded RNA. Together, these studies elucidate the structure and the catalytic activity of the Cmr1 subunit.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>24531487</pmid><doi>10.1107/S1399004713030290</doi><tpages>9</tpages></addata></record> |
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| ispartof | Acta crystallographica. Section D, Biological crystallography., 2014-02, Vol.70 (2), p.535-543 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Archaeal Proteins - chemistry Archaeal Proteins - genetics Archaeal Proteins - metabolism Archaeoglobus fulgidus Archaeoglobus fulgidus - chemistry Archaeoglobus fulgidus - immunology Archaeoglobus fulgidus - virology Bacteriology Binding Sites Clustered Regularly Interspaced Short Palindromic Repeats - genetics Clustered Regularly Interspaced Short Palindromic Repeats - immunology Cmr interference complex Cmr1 subunit Crystal structure Crystallography, X-Ray Escherichia coli - genetics Escherichia coli - metabolism Ferredoxins - chemistry Ferredoxins - genetics Ferredoxins - metabolism Host-Pathogen Interactions Models, Molecular Molecular Sequence Data Protein Structure, Secondary Protein Structure, Tertiary Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Pyrococcus furiosus - chemistry Pyrococcus furiosus - genetics Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism RNA, Viral - chemistry RNA, Viral - metabolism RNA-binding site Sequence Alignment Structural Homology, Protein Substrate Specificity |
| title | Crystal structure and CRISPR RNA-binding site of the Cmr1 subunit of the Cmr interference complex |
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