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-Structure paper
タイトル | Survey of large protein complexes in D. vulgaris reveals great structural diversity. |
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ジャーナル・号・ページ | Proc Natl Acad Sci U S A, Vol. 106, Issue 39, Page 16580-16585, Year 2009 |
掲載日 | 2009年9月29日 |
著者 | Bong-Gyoon Han / Ming Dong / Haichuan Liu / Lauren Camp / Jil Geller / Mary Singer / Terry C Hazen / Megan Choi / H Ewa Witkowska / David A Ball / Dieter Typke / Kenneth H Downing / Maxim Shatsky / Steven E Brenner / John-Marc Chandonia / Mark D Biggin / Robert M Glaeser / |
PubMed 要旨 | An unbiased survey has been made of the stable, most abundant multi-protein complexes in Desulfovibrio vulgaris Hildenborough (DvH) that are larger than Mr approximately 400 k. The quaternary ...An unbiased survey has been made of the stable, most abundant multi-protein complexes in Desulfovibrio vulgaris Hildenborough (DvH) that are larger than Mr approximately 400 k. The quaternary structures for 8 of the 16 complexes purified during this work were determined by single-particle reconstruction of negatively stained specimens, a success rate approximately 10 times greater than that of previous "proteomic" screens. In addition, the subunit compositions and stoichiometries of the remaining complexes were determined by biochemical methods. Our data show that the structures of only two of these large complexes, out of the 13 in this set that have recognizable functions, can be modeled with confidence based on the structures of known homologs. These results indicate that there is significantly greater variability in the way that homologous prokaryotic macromolecular complexes are assembled than has generally been appreciated. As a consequence, we suggest that relying solely on previously determined quaternary structures for homologous proteins may not be sufficient to properly understand their role in another cell of interest. |
リンク | Proc Natl Acad Sci U S A / PubMed:19805340 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 15.0 - 29.0 Å |
構造データ | EMDB-5041: EMDB-5042: EMDB-5043: EMDB-5044: EMDB-5045: EMDB-5046: EMDB-5047: |
由来 |
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