Structural similarity of a developmentally regulated bacterial spore coat protein to beta gamma-crystallins of the vertebrate eye lens
The solution structure of Ca(2+)-loaded protein S (M(r) 18,792) from the Gram-negative soil bacterium Myxococcus xanthus has been determined by multidimensional heteronuclear NMR spectroscopy. Protein S consists of four internally homologous motifs, arranged to produce two domains with a pseudo-twof...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1994-05, Vol.91 (10), p.4308-4312 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Bagby, S Harvey, T S Eagle, S G Inouye, S Ikura, M |
| description | The solution structure of Ca(2+)-loaded protein S (M(r) 18,792) from the Gram-negative soil bacterium Myxococcus xanthus has been determined by multidimensional heteronuclear NMR spectroscopy. Protein S consists of four internally homologous motifs, arranged to produce two domains with a pseudo-twofold symmetry axis, overall resembling a triangular prism. Each domain consists of two topologically inequivalent "Greek keys": the second and fourth motifs form standard Greek keys, whereas the first and third motifs each contain a regular alpha-helix in addition to the usual four beta-strands. The structure of protein S is similar to those of the vertebrate eye lens beta gamma-crystallins, which are thought to be evolutionarily related to protein S. Both protein S and the beta gamma-crystallins function by forming stable multimolecular assemblies. However, protein S possesses distinctive motif organization and domain packing, indicating a different mode of oligomerization and a divergent evolutionary pathway from the beta gamma-crystallins. |
| doi_str_mv | 10.1073/pnas.91.10.4308 |
| format | Article |
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Protein S consists of four internally homologous motifs, arranged to produce two domains with a pseudo-twofold symmetry axis, overall resembling a triangular prism. Each domain consists of two topologically inequivalent "Greek keys": the second and fourth motifs form standard Greek keys, whereas the first and third motifs each contain a regular alpha-helix in addition to the usual four beta-strands. The structure of protein S is similar to those of the vertebrate eye lens beta gamma-crystallins, which are thought to be evolutionarily related to protein S. Both protein S and the beta gamma-crystallins function by forming stable multimolecular assemblies. 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Protein S consists of four internally homologous motifs, arranged to produce two domains with a pseudo-twofold symmetry axis, overall resembling a triangular prism. Each domain consists of two topologically inequivalent "Greek keys": the second and fourth motifs form standard Greek keys, whereas the first and third motifs each contain a regular alpha-helix in addition to the usual four beta-strands. The structure of protein S is similar to those of the vertebrate eye lens beta gamma-crystallins, which are thought to be evolutionarily related to protein S. Both protein S and the beta gamma-crystallins function by forming stable multimolecular assemblies. However, protein S possesses distinctive motif organization and domain packing, indicating a different mode of oligomerization and a divergent evolutionary pathway from the beta gamma-crystallins.</description><subject>Animals</subject><subject>Bacterial Proteins - biosynthesis</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Binding Sites</subject><subject>Calcium - metabolism</subject><subject>Crystallins - chemistry</subject><subject>Escherichia coli - metabolism</subject><subject>Lens, Crystalline - metabolism</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Molecular</subject><subject>Mutagenesis</subject><subject>Myxococcus xanthus</subject><subject>Myxococcus xanthus - growth & development</subject><subject>Myxococcus xanthus - metabolism</subject><subject>Point Mutation</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Spores, Bacterial</subject><subject>Vertebrates</subject><subject>X-Ray Diffraction</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU-P1SAUxYnRjG9G1640rJxV30BLKSRuJhP_JZO4UNeE0ssbDC0V6Iv9An5uaeY56sYVuTnnd7g3B6EXlOwp6ZqredJpL2kZ9qwh4hHaUSJpxZkkj9GOkLqrBKvZU3Se0jdCiGwFOUNngopGEr5DPz_nuJi8RO1xcqPzOrq84mCxxgMcwYd5hClr71cc4bB4nWHAvTYZotuYOUTAJuiM5xgyuAnngHvIGh_0OOrKxDVtuJvSlprvAB8hZuhjScKwAvYwpWfoidU-wfPTe4G-vnv75eZDdfvp_ceb69vKMMJyxTtb61q0DHoubcutlb20NQMBktK2bgfbCWFsT0TDWzOAFLw3ZKjrrtWam-YCvbnPnZd-hMGU08rlao5u1HFVQTv1rzK5O3UIR8WarmMFf33CY_i-QMpqdMmA93qCsCRFOW9q0tBivLo3mhhSimAfvqBEbcWprTgl6TZvxRXi5d-bPfhPTRX98qRv4G_1T4Cyi_cZfuTifPVfZ_MLlj2xtQ</recordid><startdate>19940510</startdate><enddate>19940510</enddate><creator>Bagby, S</creator><creator>Harvey, T S</creator><creator>Eagle, S G</creator><creator>Inouye, S</creator><creator>Ikura, M</creator><general>National Acad Sciences</general><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>C1K</scope><scope>5PM</scope></search><sort><creationdate>19940510</creationdate><title>Structural similarity of a developmentally regulated bacterial spore coat protein to beta gamma-crystallins of the vertebrate eye lens</title><author>Bagby, S ; Harvey, T S ; Eagle, S G ; Inouye, S ; Ikura, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c404t-67f2a2854eb69f56ff9b9f24e8e911525df788cfb08365cde986bc0d2275aa6c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Animals</topic><topic>Bacterial Proteins - biosynthesis</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Binding Sites</topic><topic>Calcium - metabolism</topic><topic>Crystallins - chemistry</topic><topic>Escherichia coli - metabolism</topic><topic>Lens, Crystalline - metabolism</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Molecular</topic><topic>Mutagenesis</topic><topic>Myxococcus xanthus</topic><topic>Myxococcus xanthus - growth & development</topic><topic>Myxococcus xanthus - metabolism</topic><topic>Point Mutation</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Spores, Bacterial</topic><topic>Vertebrates</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bagby, S</creatorcontrib><creatorcontrib>Harvey, T S</creatorcontrib><creatorcontrib>Eagle, S G</creatorcontrib><creatorcontrib>Inouye, S</creatorcontrib><creatorcontrib>Ikura, M</creatorcontrib><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>Environmental Sciences and Pollution Management</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bagby, S</au><au>Harvey, T S</au><au>Eagle, S G</au><au>Inouye, S</au><au>Ikura, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural similarity of a developmentally regulated bacterial spore coat protein to beta gamma-crystallins of the vertebrate eye lens</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1994-05-10</date><risdate>1994</risdate><volume>91</volume><issue>10</issue><spage>4308</spage><epage>4312</epage><pages>4308-4312</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The solution structure of Ca(2+)-loaded protein S (M(r) 18,792) from the Gram-negative soil bacterium Myxococcus xanthus has been determined by multidimensional heteronuclear NMR spectroscopy. Protein S consists of four internally homologous motifs, arranged to produce two domains with a pseudo-twofold symmetry axis, overall resembling a triangular prism. Each domain consists of two topologically inequivalent "Greek keys": the second and fourth motifs form standard Greek keys, whereas the first and third motifs each contain a regular alpha-helix in addition to the usual four beta-strands. The structure of protein S is similar to those of the vertebrate eye lens beta gamma-crystallins, which are thought to be evolutionarily related to protein S. Both protein S and the beta gamma-crystallins function by forming stable multimolecular assemblies. However, protein S possesses distinctive motif organization and domain packing, indicating a different mode of oligomerization and a divergent evolutionary pathway from the beta gamma-crystallins.</abstract><cop>United States</cop><pub>National Acad Sciences</pub><pmid>8183906</pmid><doi>10.1073/pnas.91.10.4308</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Animals Bacterial Proteins - biosynthesis Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Binding Sites Calcium - metabolism Crystallins - chemistry Escherichia coli - metabolism Lens, Crystalline - metabolism Magnetic Resonance Spectroscopy Models, Molecular Mutagenesis Myxococcus xanthus Myxococcus xanthus - growth & development Myxococcus xanthus - metabolism Point Mutation Protein Conformation Protein Structure, Secondary Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Spores, Bacterial Vertebrates X-Ray Diffraction |
| title | Structural similarity of a developmentally regulated bacterial spore coat protein to beta gamma-crystallins of the vertebrate eye lens |
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