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TitleSurvey of large protein complexes in D. vulgaris reveals great structural diversity.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 106, Issue 39, Page 16580-16585, Year 2009
Publish dateSep 29, 2009
AuthorsBong-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 AbstractAn 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.
External linksProc Natl Acad Sci U S A / PubMed:19805340 / PubMed Central
MethodsEM (single particle)
Resolution15.0 - 29.0 Å
Structure data

EMDB-5041:
Ribosome structure : Structural survey of large protein complexes in Desulfovibrio vulgaris Hildenborough (DvH)
Method: EM (single particle) / Resolution: 24.0 Å

EMDB-5042:
Lumazine synthase structure : Structural survey of large protein complexes in Desulfovibrio vulgaris Hildenborough (DvH)
Method: EM (single particle) / Resolution: 15.0 Å

EMDB-5043:
GroEL structure : Structural survey of large protein complexes in Desulfovibrio vulgaris Hildenborough (DvH)
Method: EM (single particle) / Resolution: 21.0 Å

EMDB-5044:
RNA polymerase structure : Structural survey of large protein complexes in Desulfovibrio vulgaris Hildenborough (DvH)
Method: EM (single particle) / Resolution: 19.0 Å

EMDB-5045:
Phosphoenolpyruvate synthase structure : Structural survey of large protein complexes in Desulfovibrio vulgaris Hildenborough (DvH)
Method: EM (single particle) / Resolution: 29.0 Å

EMDB-5046:
Putative protein structure : Structural survey of large protein complexes in Desulfovibrio vulgaris Hildenborough (DvH)
Method: EM (single particle) / Resolution: 23.0 Å

EMDB-5047:
Inosine-5-monophosphate dehydrogenase structure : Structural survey of large protein complexes in Desulfovibrio vulgaris Hildenborough (DvH)
Method: EM (single particle) / Resolution: 19.0 Å

Source
  • Desulfovibrio vulgaris (bacteria)
  • Desulfovibrio vulgaris str. Hildenborough (bacteria)

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