Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer
The crystal structure of a polypeptide chain fragment from the surface layer protein tetrabrachion from Staphylothermus marinus has been determined at 1.8 Å resolution. As proposed on the basis of the presence of 11-residue repeats, the polypeptide chain fragment forms a parallel right-handed coiled...
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| Veröffentlicht in: | Nature structural & molecular biology 2000-09, Vol.7 (9), p.772-776 |
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| container_title | Nature structural & molecular biology |
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| creator | Stetefeld, Jörg Kammerer, Richard A Jenny, Margrit Schulthess, Therese Landwehr, Ruth Engel, Jürgen |
| description | The crystal structure of a polypeptide chain fragment from the surface layer protein tetrabrachion from Staphylothermus marinus has been determined at 1.8 Å resolution. As proposed on the basis of the presence of 11-residue repeats, the polypeptide chain fragment forms a parallel right-handed coiled coil structure. Complementary hydrophobic interactions and complex networks of surface salt bridges result in an extremely thermostable tetrameric structure with remarkable properties. In marked contrast to left-handed coiled coil tetramers, the right-handed coiled coil reveals large hydrophobic cavities that are filled with water molecules. As a consequence, the packing of the hydrophobic core differs markedly from that of a right-handed parallel coiled coil tetramer that was designed on the basis of left-handed coiled coil structures. |
| doi_str_mv | 10.1038/79006 |
| format | Article |
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As proposed on the basis of the presence of 11-residue repeats, the polypeptide chain fragment forms a parallel right-handed coiled coil structure. Complementary hydrophobic interactions and complex networks of surface salt bridges result in an extremely thermostable tetrameric structure with remarkable properties. In marked contrast to left-handed coiled coil tetramers, the right-handed coiled coil reveals large hydrophobic cavities that are filled with water molecules. 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Academic</collection><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stetefeld, Jörg</au><au>Kammerer, Richard A</au><au>Jenny, Margrit</au><au>Schulthess, Therese</au><au>Landwehr, Ruth</au><au>Engel, Jürgen</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer</atitle><jtitle>Nature structural & molecular biology</jtitle><addtitle>Nat Struct Biol</addtitle><date>2000-09</date><risdate>2000</risdate><volume>7</volume><issue>9</issue><spage>772</spage><epage>776</epage><pages>772-776</pages><issn>1072-8368</issn><issn>1545-9993</issn><eissn>2331-365X</eissn><eissn>1545-9985</eissn><abstract>The crystal structure of a polypeptide chain fragment from the surface layer protein tetrabrachion from Staphylothermus marinus has been determined at 1.8 Å resolution. 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| ispartof | Nature structural & molecular biology, 2000-09, Vol.7 (9), p.772-776 |
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| subjects | Amino Acid Sequence Crystallography, X-Ray Desulfurococcaceae - chemistry Endopeptidases - metabolism Models, Molecular Peptide Fragments - chemistry Peptide Fragments - metabolism Protein Binding Protein Structure, Quaternary Protein Structure, Secondary Sequence Alignment Staphylothermus marinus Static Electricity Water - metabolism |
| title | Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer |
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