EMD-1637
Proteome organization in a genome-reduced bacterium -Topoisomerase of Mycoplasma pneumoniae -
EMD-1637
Single-particle21.5 Å
Deposition: 03/08/2009Map released: 11/06/2010
Last modified: 11/06/2010
Sample Organism:
Mycoplasma pneumoniae
Sample: Topoisomerase from Mycoplasma pneumoniae
Deposition Authors: Kuhner S, vanNoort V, Betts MJ
,
Leo-Macias A,
Batisse C ,
Rode M,
Yamada T,
Maier T,
Bader S,
Beltran-Alvarez P ,
Castano-Diez D ,
Chen W-H ,
Devos D ,
Guell Cargol M ,
Norambuena T ,
Racke I,
Rybin V,
Schmidt A,
Yus E,
Aebersold R,
Herrmann R,
Bottcher B ,
Frangakis AS ,
Russell RB ,
Serrano L ,
Bork P,
Gavin A-C
Sample: Topoisomerase from Mycoplasma pneumoniae
Deposition Authors: Kuhner S, vanNoort V, Betts MJ
,
Leo-Macias A,
Batisse C ,
Rode M,
Yamada T,
Maier T,
Bader S,
Beltran-Alvarez P ,
Castano-Diez D ,
Chen W-H ,
Devos D ,
Guell Cargol M ,
Norambuena T ,
Racke I,
Rybin V,
Schmidt A,
Yus E,
Aebersold R,
Herrmann R,
Bottcher B ,
Frangakis AS ,
Russell RB ,
Serrano L ,
Bork P,
Gavin A-C
Proteome organization in a genome-reduced bacterium.
Kuhner S,
van Noort V ,
Betts MJ ,
Leo-Macias A,
Batisse C ,
Rode M,
Yamada T,
Maier T,
Bader S,
Beltran-Alvarez P ,
Castano-Diez D ,
Chen W-H ,
Devos D ,
Guell Cargol M ,
Norambuena T ,
Racke I,
Rybin V,
Schmidt A,
Yus E,
Aebersold R,
Herrmann R,
Bottcher B ,
Frangakis AS ,
Russell RB ,
Serrano L ,
Bork P,
Gavin A-C
(2009) Science , 326 , 1235 - 1240
,
Betts MJ ,
Leo-Macias A,
Batisse C ,
Rode M,
Yamada T,
Maier T,
Bader S,
Beltran-Alvarez P ,
Castano-Diez D ,
Chen W-H ,
Devos D ,
Guell Cargol M ,
Norambuena T ,
Racke I,
Rybin V,
Schmidt A,
Yus E,
Aebersold R,
Herrmann R,
Bottcher B ,
Frangakis AS ,
Russell RB ,
Serrano L ,
Bork P,
Gavin A-C
(2009) Science , 326 , 1235 - 1240
Abstract:
The genome of Mycoplasma pneumoniae is among the smallest found in self-replicating organisms. To study the basic principles of bacterial proteome organization, we used tandem affinity purification-mass spectrometry (TAP-MS) in a proteome-wide screen. The analysis revealed 62 homomultimeric and 116 heteromultimeric soluble protein complexes, of which the majority are novel. About a third of the heteromultimeric complexes show higher levels of proteome organization, including assembly into larger, multiprotein complex entities, suggesting sequential steps in biological processes, and extensive sharing of components, implying protein multifunctionality. Incorporation of structural models for 484 proteins, single-particle electron microscopy, and cellular electron tomograms provided supporting structural details for this proteome organization. The data set provides a blueprint of the minimal cellular machinery required for life.
The genome of Mycoplasma pneumoniae is among the smallest found in self-replicating organisms. To study the basic principles of bacterial proteome organization, we used tandem affinity purification-mass spectrometry (TAP-MS) in a proteome-wide screen. The analysis revealed 62 homomultimeric and 116 heteromultimeric soluble protein complexes, of which the majority are novel. About a third of the heteromultimeric complexes show higher levels of proteome organization, including assembly into larger, multiprotein complex entities, suggesting sequential steps in biological processes, and extensive sharing of components, implying protein multifunctionality. Incorporation of structural models for 484 proteins, single-particle electron microscopy, and cellular electron tomograms provided supporting structural details for this proteome organization. The data set provides a blueprint of the minimal cellular machinery required for life.