title: Survey of large protein complexes in D. vulgaris reveals great structural diversity.
abstract: 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.
authors.affiliation: Life Sciences, Genomics, Earth Sciences, and Physical Biosciences Divisions, Lawrence Berkeley National Laboratory, University of California, Berkeley, CA 94720, USA.
authors.forename: Bong-Gyoon
authors.initials: BG
authors.lastname: Han
authors.forename: Ming
authors.initials: M
authors.lastname: Dong
authors.forename: Haichuan
authors.initials: H
authors.lastname: Liu
authors.forename: Lauren
authors.initials: L
authors.lastname: Camp
authors.forename: Jil
authors.initials: J
authors.lastname: Geller
authors.forename: Mary
authors.initials: M
authors.lastname: Singer
authors.forename: Terry C
authors.initials: TC
authors.lastname: Hazen
authors.forename: Megan
authors.initials: M
authors.lastname: Choi
authors.forename: H Ewa
authors.initials: HE
authors.lastname: Witkowska
authors.forename: David A
authors.initials: DA
authors.lastname: Ball
authors.forename: Dieter
authors.initials: D
authors.lastname: Typke
authors.forename: Kenneth H
authors.initials: KH
authors.lastname: Downing
authors.forename: Maxim
authors.initials: M
authors.lastname: Shatsky
authors.forename: Steven E
authors.initials: SE
authors.lastname: Brenner
authors.forename: John-Marc
authors.initials: JM
authors.lastname: Chandonia
authors.forename: Mark D
authors.initials: MD
authors.lastname: Biggin
authors.forename: Robert M
authors.initials: RM
authors.lastname: Glaeser
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D018360:Crystallography, X-Ray; D030562:Databases, Protein; D016969:Desulfovibrio vulgaris / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; D046912:Multiprotein Complexes