Recombinant portal protein from Staphylococcus epidermidis bacteriophage CNPH82 is a 13-subunit oligomer
The portal protein cn3 of bacteriophage CNPH82 is predicted to serve as a gateway for translocation of viral genome into preformed pro‐capsid, like portal proteins from other double‐stranded DNA tailed bacteriophages. The host of bacteriophage CNPH82 is the opportunistic human pathogenic bacterium S...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2012-10, Vol.68 (10), p.1267-1270 |
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| container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
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| creator | Luan, Weisha Fesseler, Jochen Chechik, Maria Buttner, Carina R. Antson, Alfred A. Smits, Callum |
| description | The portal protein cn3 of bacteriophage CNPH82 is predicted to serve as a gateway for translocation of viral genome into preformed pro‐capsid, like portal proteins from other double‐stranded DNA tailed bacteriophages. The host of bacteriophage CNPH82 is the opportunistic human pathogenic bacterium Staphylococcus epidermidis, a major cause of nosocomial infections. The portal protein of this phage has been cloned, overexpressed and purified. Size‐exclusion chromatography–multi‐angle laser light scattering analysis has indicated that the portal protein contains ∼13 subunits. Crystals of the portal protein, diffracting to 4.2 Å, have been obtained. These crystals belong to the space group C2221 with the unit‐cell parameters of a = 252.4, b = 367.0, c = 175.5 Å. The self‐rotation function revealed the presence of a single 13‐subunit oligomer in the asymmetric unit. |
| doi_str_mv | 10.1107/S1744309112037645 |
| format | Article |
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The self‐rotation function revealed the presence of a single 13‐subunit oligomer in the asymmetric unit.</description><identifier>ISSN: 1744-3091</identifier><identifier>EISSN: 1744-3091</identifier><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S1744309112037645</identifier><identifier>PMID: 23027764</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>bacteriophage CNPH82 ; Crystallization Communications ; Diffraction ; DNA translocation ; Microbiology ; Minerals ; oligomeric state ; portal protein ; Protein Subunits - chemistry ; Proteins ; Recombinant Proteins - chemistry ; Staphylococcus epidermidis ; Staphylococcus epidermidis - virology ; Staphylococcus Phages - chemistry ; Viral Proteins - chemistry</subject><ispartof>Acta crystallographica. 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Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>The portal protein cn3 of bacteriophage CNPH82 is predicted to serve as a gateway for translocation of viral genome into preformed pro‐capsid, like portal proteins from other double‐stranded DNA tailed bacteriophages. The host of bacteriophage CNPH82 is the opportunistic human pathogenic bacterium Staphylococcus epidermidis, a major cause of nosocomial infections. The portal protein of this phage has been cloned, overexpressed and purified. Size‐exclusion chromatography–multi‐angle laser light scattering analysis has indicated that the portal protein contains ∼13 subunits. Crystals of the portal protein, diffracting to 4.2 Å, have been obtained. These crystals belong to the space group C2221 with the unit‐cell parameters of a = 252.4, b = 367.0, c = 175.5 Å. The self‐rotation function revealed the presence of a single 13‐subunit oligomer in the asymmetric unit.</description><subject>bacteriophage CNPH82</subject><subject>Crystallization Communications</subject><subject>Diffraction</subject><subject>DNA translocation</subject><subject>Microbiology</subject><subject>Minerals</subject><subject>oligomeric state</subject><subject>portal protein</subject><subject>Protein Subunits - chemistry</subject><subject>Proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Staphylococcus epidermidis</subject><subject>Staphylococcus epidermidis - virology</subject><subject>Staphylococcus Phages - chemistry</subject><subject>Viral Proteins - chemistry</subject><issn>1744-3091</issn><issn>1744-3091</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFv1DAQhSMEoqXwA7igSFy4BGxPHNsXpCpiW1BV0BZUcbIcZ3bXJYmDnQD77_Fqy6rAoSdb4--98bzJsueUvKaUiDdXVJQlEEUpIyCqkj_IjnelYld7eOd-lD2J8YYQAFXJx9kRA8JEEhxnmyVa3zduMMOUjz5MpsvH4Cd0Q74Kvs-vJjNutp233to55ji6FkPvWhfzxtgJg_Pjxqwxry8_nUuWp7rJKRRxbubBTbnv3Nr3GJ5mj1ami_js9jzJvizefa7Pi4uPZ-_r04vCcsJVUVbCSEUYW5mykivVSAYMFTcSGo6tpIqj4dIogZaRFlQDIE1pFRpoMVEn2du97zg3PbYWhymYTo_B9SZstTdO__0yuI1e-x8aSkVSy2Tw6tYg-O8zxkn3LlrsOjOgn6NOYXPGBAh2P0okY1BVdIe-_Ae98XMYUhKaAgDlZZozUXRP2eBjDLg6_JsSvVu5_m_lSfPi7sAHxZ8dJ0DtgZ-uw-39jvr064ItrjkIlbTFXuvihL8OWhO-6SpFwPX15ZmuRb0k1fKDFvAbzIrF8w</recordid><startdate>201210</startdate><enddate>201210</enddate><creator>Luan, Weisha</creator><creator>Fesseler, Jochen</creator><creator>Chechik, Maria</creator><creator>Buttner, Carina R.</creator><creator>Antson, Alfred A.</creator><creator>Smits, Callum</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>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201210</creationdate><title>Recombinant portal protein from Staphylococcus epidermidis bacteriophage CNPH82 is a 13-subunit oligomer</title><author>Luan, Weisha ; Fesseler, Jochen ; Chechik, Maria ; Buttner, Carina R. ; Antson, Alfred A. ; Smits, Callum</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5059-467a89022fa468f9b8232e95a83b5ed8195ea58a97ec20d39b338a4c9ea3dea83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>bacteriophage CNPH82</topic><topic>Crystallization Communications</topic><topic>Diffraction</topic><topic>DNA translocation</topic><topic>Microbiology</topic><topic>Minerals</topic><topic>oligomeric state</topic><topic>portal protein</topic><topic>Protein Subunits - chemistry</topic><topic>Proteins</topic><topic>Recombinant Proteins - chemistry</topic><topic>Staphylococcus epidermidis</topic><topic>Staphylococcus epidermidis - virology</topic><topic>Staphylococcus Phages - chemistry</topic><topic>Viral Proteins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Luan, Weisha</creatorcontrib><creatorcontrib>Fesseler, Jochen</creatorcontrib><creatorcontrib>Chechik, Maria</creatorcontrib><creatorcontrib>Buttner, Carina R.</creatorcontrib><creatorcontrib>Antson, Alfred A.</creatorcontrib><creatorcontrib>Smits, Callum</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. 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| subjects | bacteriophage CNPH82 Crystallization Communications Diffraction DNA translocation Microbiology Minerals oligomeric state portal protein Protein Subunits - chemistry Proteins Recombinant Proteins - chemistry Staphylococcus epidermidis Staphylococcus epidermidis - virology Staphylococcus Phages - chemistry Viral Proteins - chemistry |
| title | Recombinant portal protein from Staphylococcus epidermidis bacteriophage CNPH82 is a 13-subunit oligomer |
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