@article {4920,
	title = {Computational design of self-assembling protein nanomaterials with atomic level accuracy.},
	journal = {Science},
	volume = {336},
	year = {2012},
	month = {2012 Jun 1},
	pages = {1171-4},
	abstract = {<p>We describe a general computational method for designing proteins that self-assemble to a desired symmetric architecture. Protein building blocks are docked together symmetrically to identify complementary packing arrangements, and low-energy protein-protein interfaces are then designed between the building blocks in order to drive self-assembly. We used trimeric protein building blocks to design a 24-subunit, 13-nm diameter complex with octahedral symmetry and a 12-subunit, 11-nm diameter complex with tetrahedral symmetry. The designed proteins assembled to the desired oligomeric states in solution, and the crystal structures of the complexes revealed that the resulting materials closely match the design models. The method can be used to design a wide variety of self-assembling protein nanomaterials.</p>
},
	issn = {1095-9203},
	doi = {10.1126/science.1219364},
	author = {King, Neil P and Sheffler, William and Sawaya, Michael R and Vollmar, Breanna S and Sumida, John P and Andr{\'e}, Ingemar and Gonen, Tamir and Yeates, Todd O and Baker, David}
}
@article {3635,
	title = {Interactions of the transmembrane polymeric rings of the Salmonella enterica serovar Typhimurium type III secretion system.},
	journal = {mBio},
	volume = {1},
	year = {2010},
	month = {2010},
	abstract = {<p>The type III secretion system (T3SS) is an interspecies protein transport machine that plays a major role in interactions of Gram-negative bacteria with animals and plants by delivering bacterial effector proteins into host cells. T3SSs span both membranes of Gram-negative bacteria by forming a structure of connected oligomeric rings termed the needle complex (NC). Here, the localization of subunits in the Salmonella enterica serovar Typhimurium T3SS NC were probed via mass spectrometry-assisted identification of chemical cross-links in intact NC preparations. Cross-links between amino acids near the amino terminus of the outer membrane ring component InvG and the carboxyl terminus of the inner membrane ring component PrgH and between the two inner membrane components PrgH and PrgK allowed for spatial localization of the three ring components within the electron density map structures of NCs. Mutational and biochemical analysis demonstrated that the amino terminus of InvG and the carboxyl terminus of PrgH play a critical role in the assembly and function of the T3SS apparatus. Analysis of an InvG mutant indicates that the structure of the InvG oligomer can affect the switching of the T3SS substrate to translocon and effector components. This study provides insights into how structural organization of needle complex base components promotes T3SS assembly and function.</p>
},
	keywords = {Bacterial Proteins, Membrane Transport Proteins, Models, Molecular, Protein Binding, Protein Multimerization, Salmonella typhimurium},
	issn = {2150-7511},
	doi = {10.1128/mBio.00158-10},
	author = {Sanowar, Sarah and Singh, Pragya and Pfuetzner, Richard A and Andr{\'e}, Ingemar and Zheng, Hongjin and Spreter, Thomas and Strynadka, Natalie C J and Gonen, Tamir and Baker, David and Goodlett, David R and Miller, Samuel I}
}
