Survey of large protein complexes D. vulgaris reveals great structural diversity

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An unbiased survey has been made of the stable, most abundant multi-protein complexes in Desulfovibrio vulgaris Hildenborough (DvH) that are larger than Mr {approx} 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 {approx}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, ... continued below

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Han, B.-G.; Dong, M.; Liu, H.; Camp, L.; Geller, J.; Singer, M. et al. August 15, 2009.

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An unbiased survey has been made of the stable, most abundant multi-protein complexes in Desulfovibrio vulgaris Hildenborough (DvH) that are larger than Mr {approx} 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 {approx}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.

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  • Journal Name: National Academy of Sciences (PNAS); Journal Volume: 106; Journal Issue: 39; Related Information: Journal Publication Date: 2009

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  • Report No.: LBNL-2646E
  • Grant Number: DE-AC02-05CH11231
  • DOI: 10.1073/pnas.0813068106 | External Link
  • Office of Scientific & Technical Information Report Number: 973691
  • Archival Resource Key: ark:/67531/metadc927566

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  • August 15, 2009

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  • Nov. 13, 2016, 7:26 p.m.

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  • Sept. 29, 2017, 5:58 p.m.

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Han, B.-G.; Dong, M.; Liu, H.; Camp, L.; Geller, J.; Singer, M. et al. Survey of large protein complexes D. vulgaris reveals great structural diversity, article, August 15, 2009; Berkeley, California. (digital.library.unt.edu/ark:/67531/metadc927566/: accessed November 18, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.